Certificate of analysis raises a handful of sensible questions. This page answers them in order, starting with the fundamentals and moving to applications.
This page was last updated on 2026-08-01 and is reviewed periodically as new material appears.
当时的短肽研究普遍关注能否穿越血脑屏障、在低剂量下产生中枢效应，Semax 属于这一路线。鼻内给药是其主要使用方式，俄语文献报道的适应症涵盖缺血性卒中、短暂性脑缺血发作、认知功能减退以及视神经病变。这些研究大多发表在当地期刊上，样本规模与终点设置同西方试验惯例存在差异，国际同行对其临床证据的强度看法不一。
各国监管态度分化明显。俄罗斯按处方药管理，部分东欧国家留有使用记录；欧盟与美国未批准其作为药物上市，市面流通品通常标注为研究用化学品。身份差异意味着标示含量、纯度与无菌性缺少统一核查。体育领域还牵涉反兴奋剂名录，跨境携带则受目的地药品法规约束。
Semax 是人工设计的七肽，序列为 Met-Glu-His-Phe-Pro-Gly-Pro，骨架取自促肾上腺皮质激素片段 ACTH(4-10)。它于二十世纪八十年代在苏联的分子遗传学研究机构内合成。设计目标是保留该片段与注意力和记忆相关的活性，同时剔除促皮质激素释放等内分泌作用。此后俄罗斯将其登记为药品并进入临床使用。
Semax binds to melanocortin receptors and is thought to influence neuronal survival and plasticity rather than to act through the adrenal axis. Laboratory work has shown increased expression of brain-derived neurotrophic factor and nerve growth factor in treated tissue. Changes in c-Fos, a marker of neuronal activation, have also been reported. Because the peptide is rapidly degraded by peptidases, its effects are generally attributed to downstream signaling cascades rather than to sustained receptor occupancy.
Published studies are dominated by animal models of stroke, ischemia, and cognitive impairment, with a smaller number of human trials conducted in Russia. Many of the human reports are small, single-center, and published in Russian-language journals, which limits independent scrutiny. Outcome measures vary between studies and often rely on clinician-rated scales rather than objective biomarkers. Systematic reviews have noted the methodological weaknesses and called for larger, preregistered trials before firm conclusions can be drawn.
| Property | Value | Notes |
|---|---|---|
| 结构类别 | 线性合成七肽 | 无环化结构，不含二硫键 |
| 氨基酸序列 | Met-Glu-His-Phe-Pro-Gly-Pro | N 端为甲硫氨酸 |
| 分子量 | 约 814 Da | 游离碱形式的计算值 |
| 外观 | 白色至类白色粉末 | 具吸湿性 |
| 溶解性 | 易溶于水 | 亦可溶于甲醇等极性溶剂 |
Semax is a synthetic peptide created in the Soviet Union during the early 1980s by researchers working in Moscow. It was built from the short adrenocorticotropic hormone fragment known as ACTH(4-10), and the chain was then extended with three additional amino acids. The resulting molecule was named semax and entered clinical use in Russia in 1994. It is generally described as a nootropic and neuroprotective agent rather than as a hormone analogue.
The parent fragment ACTH(4-10) carries the sequence Met-Glu-His-Phe-Arg-Trp-Gly. Semax replaces the arginine and tryptophan positions with a proline-glycine-proline tail, giving Met-Glu-His-Phe-Pro-Gly-Pro. That change removes residues associated with adrenal stimulation, so the peptide does not drive cortisol release the way full ACTH does. This distinction shapes how the compound is grouped in the literature, where it sits with neuropeptides and peptide neuromodulators rather than with corticosteroids.
Regulatory status varies sharply by country. Semax is registered for medical use in Russia, where it appears in formularies as a nasal solution, and it also holds registration in a small number of neighbouring states. It has no approval from the United States Food and Drug Administration or the European Medicines Agency, and it is not a scheduled controlled substance in most jurisdictions. Elsewhere it circulates mainly as laboratory material, so purity documentation comes from suppliers rather than from a national pharmacopoeia.
Identity and purity of semax are established with reversed-phase high-performance liquid chromatography coupled to ultraviolet detection, usually at 214 nanometres. Mass spectrometry, most often electrospray ionisation in positive mode, confirms the molecular mass and reveals truncated sequences. Amino acid analysis and peptide mapping after enzymatic digestion provide additional structural confirmation. Laboratories typically report purity as the percentage area of the main peak, a figure that does not capture isomeric or oxidised variants unless the method resolves them.
The peptide is prone to several degradation pathways. Oxidation of the methionine residue produces a sulfoxide that elutes close to the parent peak in many chromatographic systems. Hydrolysis of peptide bonds and deamidation of susceptible residues in related sequences also reduce purity over time. Lyophilised material kept dry at minus twenty degrees Celsius and shielded from light is the most stable form commonly described in laboratory practice.
Semax is a synthetic heptapeptide whose sequence is Met-Glu-His-Phe-Pro-Gly-Pro. The first four residues correspond to the ACTH(4-10) fragment, while the terminal Pro-Gly-Pro extension was added to improve metabolic stability. Its molecular formula is C37H51N9O10S and its monoisotopic mass is approximately 813.9 Da. The compound is classified as a peptide research chemical and as a registered pharmaceutical product in Russia, but it does not hold marketing approval in the European Union or the United States. Naming conventions vary across supplier catalogs.
Development of the compound took place in the Soviet Union during the 1980s, largely through peptide research groups affiliated with the Shemyakin-Ovchinnikov Institute and Moscow State University. Investigators screened fragments of adrenocorticotropic hormone for activity on the central nervous system while attempting to separate cognitive effects from hormonal ones. The shortened sequence was selected because it retained behavioral activity in animal models without stimulating corticosteroid release. Early publications described the molecule as an ACTH(4-10) analog.
Identity and purity are confirmed with reversed-phase high-performance liquid chromatography, typically monitored at 214 nanometres where the peptide bond absorbs. Mass spectrometry, either electrospray or MALDI-TOF, verifies molecular mass against the theoretical value and detects truncation or adduct formation. Amino acid analysis and peptide mapping provide additional confirmation when required. The most frequently reported impurities are deletion sequences from incomplete coupling, methionine sulfoxide from oxidation, and dimeric species formed through non-covalent aggregation. Impurity profiles depend strongly on the synthesis and purification route chosen by the producer.
Published research has focused mainly on neurological and cognitive endpoints in animal models, with proposed mechanisms involving brain-derived neurotrophic factor and related signalling pathways. A substantial share of the human data originates from a limited number of research groups, and independent replication in other countries remains sparse. Regulatory status reflects that distribution: the peptide is registered as a medicine in Russia and appears in some neighbouring markets, while elsewhere it is handled as a research chemical without approved therapeutic labelling. Questions about dose-response relationships, long-term effects, and comparability across studies are still open.
Se8 + 24 F2 → 8 SeF6 In comparison with its sulfur counterpart (sulfur hexafluoride), selenium hexafluoride (SeF6) is more reactive and is a toxic pulmonary irritant. Selenium tetrafluoride is a laboratory-scale fluorinating agent. The only stable chlorides are selenium tetrachloride (SeCl4) and selenium monochloride (Se2Cl2), which might be better known as selenium(I) chloride and is structurally analogous to disulfur dichloride. Metastable solutions of selenium dichloride can be prepared from sulfuryl chloride and selenium (reaction of the elements generates the tetrachloride instead), and constitute an important reagent in the preparation of selenium compounds (e.g. Se7). The corresponding bromides are all known, and recapitulate the same stability and structure as the chlorides. The iodides of selenium are not well known, and for a long time were believed not to exist. There is limited spectroscopic evidence that the lower iodides may form in bi-elemental solutions with nonpolar solvents, such as carbon disulfide and carbon tetrachloride; but even these appear to decompose under illumination. Some selenium oxyhalides—seleninyl fluoride (SeOF2) and selenium oxychloride (SeOCl2)—have been used as specialty solvents.
Enzymes that use a metal in the active site are called "metallo-carboxypeptidases" (EC number 3.4.17). Other carboxypeptidases that use active site serine residues are called "serine carboxypeptidases" (EC number 3.4.16). Those that use an active site cysteine are called "cysteine carboxypeptidase" (or "thiol carboxypeptidases")(EC number 3.4.18). These names do not refer to the selectivity of the amino acid that is cleaved.
In much of the British Empire, slavery was subject to abolition in 1833, throughout the United States it was abolished in 1865 as a result of the Civil War, which was fought after the attempted secession of the South in order to protect its "Peculiar Institution" (i.e. slavery). In Cuba slavery was abolished in 1886. The last country in the Americas to abolish slavery was Brazil, in 1888. Chattel slavery survived longest in the Middle East. After the trans-Atlantic slave trade had been suppressed, the ancient trans-Saharan slave trade, the Indian Ocean slave trade and the Red Sea slave trade continued to traffic slaves from the African continent to the Middle East. During the 20th century, the issue of chattel slavery was addressed and investigated globally by international bodies created by the League of Nations and the United Nations (UN), such as the Temporary Slavery Commission in 1924–1926, the Committee of Experts on Slavery in 1932, and the Advisory Committee of Experts on Slavery in 1934–1939. By the time of the UN Ad Hoc Committee on Slavery in 1950–1951, legal chattel slavery still existed only in the Arabian Peninsula: in Oman, in Qatar, in Saudi Arabia, in the Trucial States and in Yemen. Legal chattel slavery was finally abolished in the Arabian Peninsula in the 1960s: Saudi Arabia and Yemen in 1962, in Dubai in 1963, and Oman as the last in 1970. The last country to abolish slavery, Mauritania, did so in 1981.
Sources: en.wikipedia.org
In October 2013, A&W opened its first new concept restaurant, A&W Burgers Chicken Floats. The new concept focuses on fresh made-to-order food and heavily emphasizes customer service. The menu features burgers made with fresh beef and a choice of toppings, hand-breaded chicken tenders, all-beef hot dogs, and several sides. The new management gave A&W a significant boost in the number of locations, with 2017 scheduled to have more openings than closures. For 2018, A&W projected an increase in its franchising operations and opening new restaurants. In April 2019, A&W returned to Singapore after a 16-year absence, its first location being at Jewel Changi Airport. In June 2019, the A&W chain started moving its headquarters to the University of Kentucky Coldstream Research Campus in 2019. A&W announced in March 2022 that it was going to withdraw from the Thai market due to economic losses. The restaurants shut down on March 20. A franchise was given to western New York in early 2023, with three locations, the first of which in Niagara Falls, set to open between May and June of that year. There are nearly 1,000 A&W Restaurants worldwide that are owned or franchised through A Great American Brand, with approximately 475 of these restaurants located in the U.S. as of October 2024. A&W rebounded its profits in the first half of 2024, emphasis on its growth is given mainly to single-brand restaurants, as well as restaurants in less conventional locations. In November 2024, the chain announced its entrance to the Milwaukee and Madison markets in Wisconsin.
In October 1997, a pumpkin was placed on the lightning rod of McGraw Tower at Cornell University in Ithaca, New York. Due to attempts to identify the pumpkin, speculation on how it was placed, and the unknown identity of the culprit, the pumpkin acquired national news coverage as well as a dedicated website with a webcam. It was nicknamed the Great Pumpkin Mystery by some news outlets. The pumpkin stayed on the top of the tower until March 1998, when it was accidentally knocked down by a crane cage during a rehearsal for its removal. After its recovery by the university's provost, it was freeze-dried and held in a glass case in various areas of the university until it decayed fully. The pumpkin continued as a part of university legend, with its anniversary marked in 2007 and 2017 and another pumpkin placed on the tower during renovations in 2023.
=== EC 2.1.1: Methyltransferases === EC 2.1.1.1: nicotinamide N-methyltransferase EC 2.1.1.2: guanidinoacetate N-methyltransferase EC 2.1.1.3: thetin—homocysteine S-methyltransferase EC 2.1.1.4: acetylserotonin O-methyltransferase EC 2.1.1.5: betaine—homocysteine S-methyltransferase EC 2.1.1.6: catechol O-methyltransferase EC 2.1.1.7: nicotinate N-methyltransferase EC 2.1.1.8: histamine N-methyltransferase EC 2.1.1.9: thiol S-methyltransferase EC 2.1.1.10: homocysteine S-methyltransferase EC 2.1.1.11: magnesium protoporphyrin IX methyltransferase EC 2.1.1.12: methionine S-methyltransferase EC 2.1.1.13: methionine synthase EC 2.1.1.14: 5-methyltetrahydropteroyltriglutamate—homocysteine S-methyltransferase EC 2.1.1.15: fatty-acid O-methyltransferase EC 2.1.1.16: methylene-fatty-acyl-phospholipid synthase EC 2.1.1.17: phosphatidylethanolamine N-methyltransferase EC 2.1.1.18: polysaccharide O-methyltransferase EC 2.1.1.19: trimethylsulfonium—tetrahydrofolate N-methyltransferase EC 2.1.1.20: glycine N-methyltransferase EC 2.1.1.21: methylamine—glutamate N-methyltransferase EC 2.1.1.22: carnosine N-methyltransferase EC 2.1.1.23: now covered by EC 2.1.1.124, EC 2.1.1.125 and EC 2.1.1.126 EC 2.1.1.24: now covered by EC 2.1.1.77, EC 2.1.1.80 and EC 2.1.1.100 EC 2.1.1.25: phenol O-methyltransferase EC 2.1.1.26: iodophenol O-methyltransferase EC 2.1.1.27: tyramine N-methyltransferase EC 2.1.1.28: phenylethanolamine N-methyltransferase EC 2.1.1.29: Now covered by EC 2.1.1.202, EC 2.1.1.203 and EC .1.1.204 EC 2.1.1.30: tRNA (purine-2- or -6-)-methyltransferase: Reactions previously described are due to EC 2.1.1.32 EC 2.1.1.31: Now covered by EC 2.1.1.221 and EC 2.1.1.228 EC 2.1.1.32: Now covered by EC 2.1.1.213, EC 2.1.1.214, EC 2.1.1.215 and EC 2.1.1.216 EC 2.1.1.33: tRNA (guanine46-N7)-methyltransferase EC 2.1.1.34: tRNA (guanosine18-2′-O)-methyltransferase EC 2.1.1.35: tRNA (uracil54-C5)-methyltransferase EC 2.1.1.36: Now covered by EC 2.1.1.217, EC 2.1.1.218, EC 2.1.1.219, EC 2.1.1.220 EC 2.1.1.37: DNA (cytosine-5-)-methyltransferase EC 2.1.1.38: O-demethylpuromycin O-methyltransferase EC 2.1.1.39: inositol 3-methyltransferase EC 2.1.1.40: inositol 1-methyltransferase EC 2.1.1.41: sterol 24-C-methyltransferase EC 2.1.1.42: flavone 3′-O-methyltransferase EC 2.1.1.43: Now described by EC 2.1.1.354, EC 2.1.1.355, EC 2.1.1.356, EC 2.1.1.357, EC 2.1.1.358, EC 2.1.1.359, EC 2.1.1.360, EC 2.1.1.361 and EC 2.1.1.362 EC 2.1.1.44: L-histidine Nα-methyltransferase EC 2.1.1.45: thymidylate synthase EC 2.1.1.46: isoflavone 4′-O-methyltransferase EC 2.1.1.47: indolepyruvate C-methyltransferase EC 2.1.1.48: Now covered by EC 2.1.1.181, EC 2.1.1.182, EC 2.1.1.183 and EC 2.1.1.184 EC 2.1.1.49: amine N-methyltransferase EC 2.1.1.50: loganate O-methyltransferase EC 2.1.1.51: Now covered by EC 2.1.1.187 and EC 2.1.1.188 EC 2.1.1.52: Now covered by EC 2.1.1.171, EC 2.1.1.172, EC 2.1.1.173 and EC 2.1.1.174 EC 2.1.1.53: putrescine N-methyltransferase EC 2.1.1.54: deoxycytidylate C-methyltransferase EC 2.1.1.55: tRNA (adenine-N6-)-methyltransferase EC 2.1.1.56: mRNA (guanine-N7)-methyltransferase EC 2.1.1.57: methyltransferase cap1 EC 2.1.1.58: deleted, included in EC 2.1.1.57 EC 2.1.1.59: [cytochrome c]-lysine N-methyltransferase EC 2.1.1.60: calmodulin-lysine N-methyltransferase EC 2.1.1.61: tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase EC 2.1.1.62: mRNA (2′-O-methyladenosine-N6-)-methyltransferase EC 2.1.1.63: methylated-DNA—[protein]-cysteine S-methyltransferase EC 2.1.1.64: 3-demethylubiquinol 3-O-methyltransferase EC 2.1.1.65: licodione 2′-O-methyltransferase EC 2.1.1.66: Now covered by EC 2.1.1.230 EC 2.1.1.67: thiopurine S-methyltransferase EC 2.1.1.68: caffeate O-methyltransferase EC 2.1.1.69: 5-hydroxyfuranocoumarin 5-O-methyltransferase EC 2.1.1.70: 8-hydroxyfuranocoumarin 8-O-methyltransferase EC 2.1.1.71: phosphatidyl-N-methylethanolamine N-methyltransferase EC 2.1.1.72: site-specific DNA-methyltransferase (adenine-specific) EC 2.1.1.73: deleted: reaction is that of EC 2.1.1.37, DNA (cytosine-5-)-methyltransferase EC 2.1.1.74: methylenetetrahydrofolate—tRNA-(uracil54-C5)-methyltransferase [NAD(P)H-oxidizing] EC 2.1.1.75: apigenin 4′-O-methyltransferase EC 2.1.1.76: quercetin 3-O-methyltransferase EC 2.1.1.77: protein-L-isoaspartate(D-aspartate) O-methyltransferase EC 2.1.1.78: isoorientin 3′-O-methyltransferase EC 2.1.1.79: cyclopropane-fatty-acyl-phospholipid synthase EC 2.1.1.80: protein-glutamate O-methyltransferase EC 2.1.1.81: deleted, included in EC 2.1.1.49 EC 2.1.1.82: 3-methylquercetin 7-O-methyltransferase EC 2.1.1.83: 3,7-dimethylquercetin 4′-O-methyltransferase EC 2.1.1.84: methylquercetagetin 6-O-methyltransferase EC 2.1.1.85: protein-histidine N-methyltransferase EC 2.1.1.86: Now covered by EC 7.2.1.4 EC 2.1.1.87: pyridine N-methyltransferase EC 2.1.1.88: 8-hydroxyquercetin 8-O-methyltransferase EC 2.1.1.89: tetrahydrocolumbamine 2-O-methyltransferase EC 2.1.1.90: methanol—5-hydroxybenzimidazolylcobamide Co-methyltransferase EC 2.1.1.91: isobutyraldoxime O-methyltransferase EC 2.1.1.92: Now included with EC 2.1.1.69 EC 2.1.1.93: is identical to EC 2.1.1.70, 8-hydroxyfuranocoumarin 8-O-methyltransferase EC 2.1.1.94: tabersonine 16-O-methyltransferase EC 2.1.1.95: tocopherol C-methyltransferase EC 2.1.1.96: thioether S-methyltransferase EC 2.1.1.97: 3-hydroxyanthranilate 4-C-methyltransferase EC 2.1.1.98: diphthine synthase EC 2.1.1.99: 3-hydroxy-16-methoxy-2,3-dihydrotabersonine N-methyltransferase EC 2.1.1.100: protein-S-isoprenylcysteine O-methyltransferase EC 2.1.1.101: macrocin O-methyltransferase EC 2.1.1.102: demethylmacrocin O-methyltransferase EC 2.1.1.103: phosphoethanolamine N-methyltransferase EC 2.1.1.104: caffeoyl-CoA O-methyltransferase EC 2.1.1.105: N-benzoyl-4-hydroxyanthranilate 4-O-methyltransferase EC 2.1.1.106: tryptophan 2-C-methyltransferase EC 2.1.1.107: uroporphyrinogen-III C-methyltransferase EC 2.1.1.108: 6-hydroxymellein O-methyltransferase EC 2.1.1.109: demethylsterigmatocystin 6-O-methyltransferase EC 2.1.1.110: sterigmatocystin 8-O-methyltransferase EC 2.1.1.111: anthranilate N-methyltransferase EC 2.1.1.112: glucuronoxylan 4-O-methyltransferase EC 2.1.1.113: site-specific DNA-methyltransferase (cytosine-N4-specific) EC 2.1.1.114: polyprenyldihydroxybenzoate methyltransferase EC 2.1.1.115: (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline N-methyltransferase EC 2.1.1.116: 3′-hydroxy-N-methyl-(S)-coclaurine 4′-O-methyltransferase EC 2.1.1.117: (S)-scoulerine 9-O-methyltransferase EC 2.1.1.118: columbamine O-methyltransferase EC 2.1.1.119: 10-hydroxydihydrosanguinarine 10-O-methyltransferase EC 2.1.1.120: 12-hydroxydihydrochelirubine 12-O-methyltransferase EC 2.1.1.121: 6-O-methylnorlaudanosoline 5′-O-methyltransferase EC 2.1.1.122: (S)-tetrahydroprotoberberine N-methyltransferase EC 2.1.1.123: [cytochrome-c]-methionine S-methyltransferase EC 2.1.1.124: Now covered by EC 2.1.1.319, EC 2.1.1.320, EC 2.1.1.321 and EC 2.1.1.322 EC 2.1.1.125: Now covered by EC 2.1.1.319, EC 2.1.1.320 and EC 2.1.1.321 EC 2.1.1.126: Now covered by EC 2.1.1.319, EC 2.1.1.320 and EC 2.1.1.321 EC 2.1.1.127: [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase EC 2.1.1.128: (RS)-norcoclaurine 6-O-methyltransferase EC 2.1.1.129: inositol 4-methyltransferase EC 2.1.1.130: precorrin-2 C20-methyltransferase EC 2.1.1.131: precorrin-2 C17-methyltransferase EC 2.1.1.132: precorrin-6B C5,15-methyltransferase (decarboxylating) EC 2.1.1.133: precorrin-4 C11-methyltransferase EC 2.1.1.134: now with EC 2.1.1.129 EC 2.1.1.135: now EC 1.16.1.8 EC 2.1.1.136: chlorophenol O-methyltransferase EC 2.1.1.137: arsenite methyltransferase EC 2.1.1.138: deleted: Reaction due to EC 2.1.1.137 EC 2.1.1.139: 3′-demethylstaurosporine O-methyltransferase EC 2.1.1.140: (S)-coclaurine-N-methyltransferase EC 2.1.1.141: jasmonate O-methyltransferase EC 2.1.1.142: cycloartenol 24-C-methyltransferase EC 2.1.1.143: 24-methylenesterol C-methyltransferase EC 2.1.1.144: trans-aconitate 2-methyltransferase EC 2.1.1.145: trans-aconitate 3-methyltransferase EC 2.1.1.146: (iso)eugenol O-methyltransferase EC 2.1.1.147: corydaline synthase EC 2.1.1.148: thymidylate synthase (FAD) EC 2.1.1.149: Now covered by EC 2.1.1.267, flavonoid 3′,5′-methyltransferase EC 2.1.1.150: isoflavone 7-O-methyltransferase EC 2.1.1.151: cobalt-factor II C20-methyltransferase EC 2.1.1.152: precorrin-6A synthase (deacetylating) EC 2.1.1.153: vitexin 2′′-O-rhamnoside 7-O-methyltransferase EC 2.1.1.154: isoliquiritigenin 2′-O-methyltransferase EC 2.1.1.155: kaempferol 4′-O-methyltransferase EC 2.1.1.156: glycine/sarcosine N-methyltransferase EC 2.1.1.157: sarcosine/dimethylglycine N-methyltransferase EC 2.1.1.158: 7-methylxanthosine synthase EC 2.1.1.159: theobromine synthase EC 2.1.1.160: caffeine synthase EC 2.1.1.161: dimethylglycine N-methyltransferase EC 2.1.1.162: glycine/sarcosine/dimethylglycine N-methyltransferase EC 2.1.1.163: demethylmenaquinone methyltransferase EC 2.1.1.164: demethylrebeccamycin-D-glucose O-methyltransferase EC 2.1.1.165: methyl halide transferase EC 2.1.1.166: 23S rRNA (uridine2552-2′-O)-methyltransferase EC 2.1.1.167: 27S pre-rRNA (guanosine2922-2′-O)-methyltransferase EC 2.1.1.168: 21S rRNA (uridine2791-2′-O)-methyltransferase EC 2.1.1.169: tricetin 3′,4′,5′-O-trimethyltransferase EC 2.1.1.170: 16S rRNA (guanine527-N7)-methyltransferase EC 2.1.1.171: 16S rRNA (guanine966-N2)-methyltransferase EC 2.1.1.172: 16S rRNA (guanine1207-N2))-methyltransferase EC 2.1.1.173: 23S rRNA (guanine2445-N2)-methyltransferase EC 2.1.1.174: 23S rRNA (guanine1835-N2)-methyltransferase EC 2.1.1.175: tricin synthase EC 2.1.1.176: 16S rRNA (cytosine967-C5)-methyltransferase EC 2.1.1.177: 23S rRNA (pseudouridine1915-N3)-methyltransferase EC 2.1.1.178: 16S rRNA (cytosine1407-C5)-methyltransferase EC 2.1.1.179: 16S rRNA (guanine1405-N7)-methyltransferase EC 2.1.1.180: 16S rRNA (adenine1408-N1)-methyltransferase EC 2.1.1.181: 23S rRNA (adenine1618-N6)-methyltransferase EC 2.1.1.182: 16S rRNA (adenine1518-N6/adenineadenine1519-N6)-dimethyltransferase EC 2.1.1.183: 18S rRNA (adenine1779-N6/adenine1780-N6)-dimethyltransferase EC 2.1.1.184: 23S rRNA (adenine2085-N6)-dimethyltransferase EC 2.1.1.185: 23S rRNA (guanosine2251-2′-O)-methyltransferase EC 2.1.1.186: 23S rRNA (cytidine2498-2′-O)-methyltransferase EC 2.1.1.187: 23S rRNA (guanine745-N1)-methyltransferase EC 2.1.1.188: 23S rRNA (guanine748-N1)-methyltransferase EC 2.1.1.189: 23S rRNA (uracil747-C5)-methyltransferase EC 2.1.1.190: 23S rRNA (uracil1939-C5)-methyltransferase EC 2.1.1.191: 23S rRNA (cytosine1962-C5)-methyltransferase EC 2.1.1.192: 23S rRNA (adenine2503-C2)-methyltransferase EC 2.1.1.193: 16S rRNA (uracil1498-N3)-methyltransferase EC 2.1.1.194: A mixture of EC 2.1.1.192 and EC 2.1.1.224 EC 2.1.1.195: cobalt-precorrin-5B (C1)-methyltransferase EC 2.1.1.196: cobalt-precorrin-7 (C15)-methyltransferase (decarboxylating) EC 2.1.1.197: malonyl-[acyl-carrier protein] O-methyltransferase EC 2.1.1.198: 16S rRNA (cytidine1402-2′-O)-methyltransferase EC 2.1.1.199: 16S rRNA (cytosine1402-N4)-methyltransferase EC 2.1.1.200: tRNA (cytidine32/uridine32-2′-O)-methyltransferase EC 2.1.1.201: 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase EC 2.1.1.202: multisite-specific tRNA:(cytosine-C5)-methyltransferase EC 2.1.1.203: tRNA (cytosine34-C5)-methyltransferase EC 2.1.1.204: tRNA (cytosine38-C5)-methyltransferase EC 2.1.1.205: tRNA (cytidine32/guanosine34-2′-O)-methyltransferase EC 2.1.1.206: tRNA (cytidine56-2′-O)-methyltransferase EC 2.1.1.207: tRNA (cytidine34-2′-O)-methyltransferase EC 2.1.1.208: 23S rRNA (uridine2479-2′-O)-methyltransferase EC 2.1.1.209: 23S rRNA (guanine2535-N1)-methyltransferase EC 2.1.1.210: demethylspheroidene O-methyltransferase EC 2.1.1.211: tRNASer(uridine44-2′-O)-methyltransferase EC 2.1.1.212: 2,7,4′-trihydroxyisoflavanone 4′-O-methyltransferase EC 2.1.1.213: tRNA (guanine110-N2)-dimethyltransferase EC 2.1.1.214: tRNA (guanine10-N2)-methyltransferase EC 2.1.1.215: tRNA (guanine26-N2/guanine27-N2)-dimethyltransferase EC 2.1.1.216: tRNA (guanine26-N2)-dimethyltransferase EC 2.1.1.217: tRNA (adenine22-N1)-methyltransferase EC 2.1.1.218: tRNA (adenine9-N1)-methyltransferase EC 2.1.1.219: tRNA (adenine57-N1/adenine58-N1)-methyltransferase EC 2.1.1.220: tRNA (adenine58-N1)-methyltransferase EC 2.1.1.221: tRNA (guanine9-N1)-methyltransferase EC 2.1.1.222: 2-polyprenyl-6-hydroxyphenyl methylase EC 2.1.1.223: tRNA1Val (adenine937-N6)-methyltransferase EC 2.1.1.224: 23S rRNA (adenine2503-C8)-methyltransferase EC 2.1.1.225: tRNA:m4X modification enzyme EC 2.1.1.226: 23S rRNA (cytidine1920-2′-O)-methyltransferase EC 2.1.1.227: 16S rRNA (cytidine1409-2′-O)-methyltransferase EC 2.1.1.228: tRNA (guanine37-N1)-methyltransferase EC 2.1.1.229: tRNA (carboxymethyluridine34-5-O)-methyltransferase EC 2.1.1.230: 23S rRNA (adenosine1067-2′-O)-methyltransferase EC 2.1.1.231: flavonoid 4′-O-methyltransferase EC 2.1.1.232: naringenin 7-O-methyltransferase EC 2.1.1.233: [phosphatase 2A protein]-leucine-carboxy methyltransferase EC 2.1.1.234: dTDP-3-amino-3,4,6-trideoxy-α-D-glucopyranose N,N-dimethyltransferase EC 2.1.1.235: dTDP-3-amino-3,6-dideoxy-α-D-glucopyranose N,N-dimethyltransferase EC 2.1.1.236: dTDP-3-amino-3,6-dideoxy-α-D-galactopyranose N,N-dimethyltransferase EC 2.1.1.237: mycinamicin III 3′′-O-methyltransferase EC 2.1.1.238: mycinamicin VI 2′′-O-methyltransferaseD EC 2.1.1.239: L-olivosyl-oleandolide 3-O-methyltransferase EC 2.1.1.240: trans-resveratrol di-O-methyltransferase EC 2.1.1.241: 2,4,7-trihydroxy-1,4-benzoxazin-3-one-glucoside 7-O-methyltransferase EC 2.1.1.242: 16S rRNA (guanine1516-N2)-methyltransferase EC 2.1.1.243: 2-ketoarginine methyltransferase EC 2.1.1.244: protein N-terminal methyltransferase EC 2.1.1.245: 5-methyltetrahydrosarcinapterin—corrinoid/iron-sulfur protein Co-methyltransferase EC 2.1.1.246: [methyl-Co(III) methanol-specific corrinoid protein]—coenzyme M methyltransferase EC 2.1.1.247: (methyl-Co(III) methylamine-specific corrinoid protein)—coenzyme M methyltransferase EC 2.1.1.248: methylamine—corrinoid protein Co-methyltransferase EC 2.1.1.249: dimethylamine—corrinoid protein Co-methyltransferase EC 2.1.1.250: trimethylamine—corrinoid protein Co-methyltransferase EC 2.1.1.251: methylated-thiol—coenzyme M methyltransferase EC 2.1.1.252: tetramethylammonium—corrinoid protein Co-methyltransferase EC 2.1.1.253: [methyl-Co(III) tetramethylammonium-specific corrinoid protein]—coenzyme M methyltransferase EC 2.1.1.254: erythromycin 3′′-O-methyltransferase EC 2.1.1.255: geranyl diphosphate 2-C-methyltransferase EC 2.1.1.256: tRNA (guanine6-N6-methyltransferase) EC 2.1.1.257: tRNA (pseudouridine54-N1)-methyltransferase EC 2.1.1.258: 5-methyltetrahydrofolate—corrinoid/iron-sulfur protein Co-methyltransferase EC 2.1.1.259: [fructose-bisphosphate aldolase]-lysine N-methyltransferase EC 2.1.1.260: rRNA small subunit pseudouridine methyltransferase Nep1 EC 2.1.1.261: 4-dimethylallyltryptophan N-methyltransferase EC 2.1.1.262: squalene methyltransferase EC 2.1.1.263: botryococcene C-methyltransferase EC 2.1.1.264: 23S rRNA (guanine2069-N7)-methyltransferase EC 2.1.1.265: tellurite methyltransferase EC 2.1.1.266: 23S rRNA (adenine2030-N6)-methyltransferase EC 2.1.1.267: flavonoid 3′,5′-methyltransferase EC 2.1.1.268: tRNAThr (cytosine32-N3)-methyltransferase EC 2.1.1.269: dimethylsulfoniopropionate demethylase EC 2.1.1.270: (+)-6a-hydroxymaackiain 3-O-methyltransferase EC 2.1.1.271: cobalt-precorrin-4 methyltransferase EC 2.1.1.272: cobalt-factor III methyltransferase EC 2.1.1.273: benzoate O-methyltransferase EC 2.1.1.274: salicylate 1-O-methyltransferase EC 2.1.1.275: gibberellin A9 O-methyltransferase EC 2.1.1.276: gibberellin A4 carboxyl methyltransferase EC 2.1.1.277: anthranilate O-methyltransferase EC 2.1.1.278: indole-3-acetate O-methyltransferase EC 2.1.1.279: trans-anol O-methyltransferase EC 2.1.1.280: selenocysteine Se-methyltransferase EC 2.1.1.281: phenylpyruvate C3-methyltransferase EC 2.1.1.282: tRNAPhe 7-[(3-amino-3-carboxypropyl)-4-demethylwyosine37-N4]-methyltransferase EC 2.1.1.283: emodin O-methyltransferase EC 2.1.1.284: 8-demethylnovobiocic acid C8-methyltransferase EC 2.1.1.285: demethyldecarbamoylnovobiocin O-methyltransferase EC 2.1.1.286: 25S rRNA (adenine2142-N1)-methyltransferase EC 2.1.1.287: 25S rRNA (adenine645-N1)-methyltransferase EC 2.1.1.288: aklanonic acid methyltransferase EC 2.1.1.289: cobalt-precorrin-7 (C5)-methyltransferase EC 2.1.1.290: tRNAPhe [7-(3-amino-3-carboxypropyl)wyosine37-O]-methyltransferase EC 2.1.1.291: (R,S)-reticuline 7-O-methyltransferase EC 2.1.1.292: carminomycin 4-O-methyltransferase EC 2.1.1.293: 6-hydroxytryprostatin B O-methyltransferase EC 2.1.1.294: 3-O-phospho-polymannosyl GlcNAc-diphospho-ditrans,octacis-undecaprenol 3-phospho-methyltransferase EC 2.1.1.295: 2-methyl-6-phytyl-1,4-hydroquinone methyltransferase EC 2.1.1.296: methyltransferase cap2 EC 2.1.1.297: peptide chain release factor N5-glutamine methyltransferase EC 2.1.1.298: ribosomal protein L3 N5-glutamine methyltransferase EC 2.1.1.299: protein N-terminal monomethyltransferase EC 2.1.1.300: pavine N-methyltransferase EC 2.1.1.301: cypemycin N-terminal methyltransferase EC 2.1.1.302: 3-hydroxy-5-methyl-1-naphthoate 3-O-methyltransferase EC 2.1.1.303: 2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase EC 2.1.1.304: L-tyrosine C3-methyltransferase EC 2.1.1.305: 8-demethyl-8-α-L-rhamnosyltetracenomycin-C 2′-O-methyltransferase EC 2.1.1.306: 8-demethyl-8-(2-methoxy-α-L-rhamnosyl)tetracenomycin-C 3′-O-methyltransferase EC 2.1.1.307: 8-demethyl-8-(2,3-dimethoxy-α-L-rhamnosyl)tetracenomycin-C 4′-O-methyltransferase EC 2.1.1.308: cytidylyl-2-hydroxyethylphosphonate methyltransferase EC 2.1.1.309: 18S rRNA (guanine1575-N7)-methyltransferase EC 2.1.1.310: 25S rRNA (cytosine2870-C5)-methyltransferase EC 2.1.1.311: 25S rRNA (cytosine2278-C5)-methyltransferase EC 2.1.1.312: 25S rRNA (uracil2843-N3)-methyltransferase EC 2.1.1.313: 25S rRNA (uracil2634-N3)-methyltransferase EC 2.1.1.314: diphthine methyl ester synthase EC 2.1.1.315: 27-O-demethylrifamycin SV methyltransferase EC 2.1.1.316: mitomycin 6-O-methyltransferase EC 2.1.1.317: sphingolipid C9-methyltransferase EC 2.1.1.318: [trehalose-6-phosphate synthase]-L-cysteine S-methyltransferase EC 2.1.1.319: type I protein arginine methyltransferase EC 2.1.1.320: type II protein arginine methyltransferase EC 2.1.1.321: type III protein arginine methyltransferase EC 2.1.1.322: type IV protein arginine methyltransferase EC 2.1.1.323: (–)-pluviatolide 4-O-methyltransferase EC 2.1.1.324: dTDP-4-amino-2,3,4,6-tetradeoxy-D-glucose N,N-dimethyltransferase EC 2.1.1.325: juvenile hormone-III synthase EC 2.1.1.326: N-acetyldemethylphosphinothricin P-methyltransferase EC 2.1.1.327: phenazine-1-carboxylate N-methyltransferase EC 2.1.1.328: N-demethylindolmycin N-methyltransferase EC 2.1.1.329: demethylphylloquinol methyltransferase EC 2.1.1.330: 5′-demethylyatein 5′-O-methyltransferase EC 2.1.1.331: bacteriochlorophyllide d C-121-methyltransferase EC 2.1.1.332: bacteriochlorophyllide d C-82-methyltransferase EC 2.1.1.333: bacteriochlorophyllide d C-20 methyltransferase EC 2.1.1.334: methanethiol S-methyltransferase EC 2.1.1.335: 4-amino-anhydrotetracycline N4-methyltransferase EC 2.1.1.336: norbelladine O-methyltransferase EC 2.1.1.337: reticuline N-methyltransferase EC 2.1.1.338: desmethylxanthohumol 6′-O-methyltransferase EC 2.1.1.339: xanthohumol 4-O-methyltransferase EC 2.1.1.340: 3-aminomethylindole N'-methyltransferase EC 2.1.1.341: vanillate/3-O-methylgallate O-demethylase EC 2.1.1.342: anaerobilin synthase EC 2.1.1.343: 8-amino-8-demethylriboflavin N,N-dimethyltransferase EC 2.1.1.344: ornithine lipid N-methyltransferase EC 2.1.1.345: psilocybin synthase EC 2.1.1.346: U6 snRNA m6A methyltransferase EC 2.1.1.347: (+)-O-methylkolavelool synthase EC 2.1.1.348: mRNA m6A methyltransferase EC 2.1.1.349: toxoflavin synthase EC 2.1.1.350: menaquinone C8-methyltransferase EC 2.1.1.351: nocamycin O-methyltransferase EC 2.1.1.352: 3-O-acetyl-4′-O-demethylpapaveroxine 4′-O-methyltransferase EC 2.1.1.353: demethylluteothin O-methyltransferase EC 2.1.1.354: [histone H3]-lysine4 N-trimethyltransferase EC 2.1.1.355: [histone H3]-lysine9 N-trimethyltransferase EC 2.1.1.356: [histone H3]-lysine27 N-trimethyltransferase EC 2.1.1.357: [histone H3]-lysine36 N-dimethyltransferase EC 2.1.1.358: [histone H3]-dimethyl-L-lysine36 N-methyltransferase. Now known to have the activity of EC 2.1.1.359, [histone H3]-lysine36 N-trimethyltransferase. EC 2.1.1.359: [histone H3]-lysine36 N-trimethyltransferase EC 2.1.1.360: [histone H3]-lysine79 N-trimethyltransferase EC 2.1.1.361: [histone H4]-lysine20 N-methyltransferase EC 2.1.1.362: [histone H4]-N-methyl-L-lysine20 N-methyltransferase EC 2.1.1.363: pre-sodorifen synthase EC 2.1.1.364: [histone H3]-lysine4 N-methyltransferase EC 2.1.1.365: MMP 1-O-methyltransferase EC 2.1.1.366: [histone H3]-N6,N6-dimethyl-lysine9 N-methyltransferase EC 2.1.1.367: [histone H3]-lysine9 N-methyltransferase EC 2.1.1.368: [histone H3]-lysine9 N-dimethyltransferase EC 2.1.1.369: [histone H3]-lysine27 N-methyltransferase EC 2.1.1.370: [histone H3]-lysine4 N-dimethyltransferase EC 2.1.1.371: [histone H3]-lysine27 N-dimethyltransferase EC 2.1.1.372: [histone H4]-lysine20 N-trimethyltransferase EC 2.1.1.373: 2-hydroxy-4-(methylsulfanyl)butanoate S-methyltransferase EC 2.1.1.374: 2-heptyl-1-hydroxyquinolin-4(1H)-one methyltransferase EC 2.1.1.375: NNS virus cap methyltransferase EC 2.1.1.376: glycine betaine—corrinoid protein Co-methyltransferase EC 2.1.1.377: [methyl-Co(III) glycine betaine-specific corrinoid protein]—coenzyme M methyltransferase EC 2.1.1.378: [methyl-Co(III) glycine betaine-specific corrinoid protein]—tetrahydrofolate methyltransferase EC 2.1.1.379: [methyl coenzyme M reductase]-L-arginine C-5-methyltransferase
Sources: en.wikipedia.org
The town was founded in 1515 by Mani Ram, a Zamindar under the Lodhi Dynasty. By the 18th century, his descendent Gangaram Singh governed Manimajra and 84 surrounding villages as a Mughal vassal. Following the decline of Mughal authority, Gangaram's son, Gharib Dass, established the independent Manimajra State. Despite early conflicts with the Raja of Nahan, Gharib Dass expanded his territory, seizing Pinjore and establishing the Manimajra Fort as his capital. Upon his death in 1783, his son Raja Gopal Singh took over, eventually receiving the title of Raja from the British in 1814 for his service in the Gurkha campaign. Gopal Singh is notably responsible for building the Mansa Devi Temple (1811–1815). The dynasty continued through Raja Goverdhan Singh and Raja Gurbaksh Singh, ending with Raja Bhagwan Singh, who died without a male heir in 1866. Consequently, the British annexed the state, and the fort later passed to the Raja of Faridkot through marriage.
Fish vs. Cephalopods TONMO.COM – The Octopus News Magazine Online – cephalopod articles and discussion Scientific American: Can a Squid Fly Out of the Water? Roger Hanlon's Seminar: "Rapid Adaptive Camouflage and Signaling in Cephalopods"
Alexios' concentration of power in the hands of his Komnenos dynasty meant the most serious political threats came from within the imperial family—before his coronation, John II had to overcome his mother Irene and his sister Anna, and the primary threat during his reign was his brother Isaac. John campaigned annually and extensively—he fought the Pechenegs in 1122, the Hungarians in the late 1120s, and the Seljuks throughout his reign, waging large campaigns in Syria in his final years—but he did not achieve large territorial gains. In 1138, John raised the imperial standard over the Crusader Principality of Antioch to intimidate the city into allying with the Byzantines, but did not attack, fearing that it would provoke western Christendom to respond. Manuel I used the considerable financial resources left by his father in pursuit of his ambitions, and also to secure the empire's position in an increasingly multilateral geopolitical landscape. Through a combination of diplomacy and subsidies, he cultivated a network of allies and client rulers around the empire: the Turks of the Sultanate of Rum, the Kingdom of Hungary, the Cilician Armenians, Balkan princes, Italian and Dalmatian cities, and most importantly Antioch and the Crusader States, marrying one of their princesses in 1161. Manuel managed the difficult passage of the Second Crusade through Byzantine territories in 1147, but the campaign's failure was blamed on the Byzantines by western contemporaries.
Sources: en.wikipedia.org
不存在。它是依据 ACTH 的一段序列人工设计的分子，天然蛋白质中找不到与之完全相同的七肽。名称属于研究代号，而非天然物质名。
Semax 对应 ACTH 第 4 至第 10 位的片段，并在两端做了替换与延长，使其不再具备促肾上腺皮质激素的典型内分泌活性。这一改动同时改变了它在体内的稳定性与分布特征。
俄罗斯将其列为处方药物，需要医生开具处方。多数其他国家把它当作研究化合物，不能作为药品销售或宣称疗效。具体合法性取决于当地法规。
It is associated with the melanocortin receptor family, particularly subtypes found in the central nervous system. This interaction is separate from the adrenal pathway activated by full-length ACTH.