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Merck
CN

04685

Nε-甲基-L-赖氨酸 盐酸盐

≥98.0% (TLC)

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关于此项目

经验公式(希尔记法):
C7H16N2O2 · HCl
化学文摘社编号:
分子量:
196.68
EC 号:
MDL编号:
UNSPSC代码:
12352202
PubChem化学物质编号:
NACRES:
NA.32
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质量水平

方案

≥98.0% (TLC)

旋光性

[α]/D 20.5±1.5°, c = 0.1 in 1 M HCl

储存温度

2-8°C

SMILES字符串

Cl.CNCCCC[C@H](N)C(O)=O
Cl.CNCCCC[C@H](N)C(O)=O

InChI

1S/C7H16N2O2.ClH/c1-9-5-3-2-4-6(8)7(10)11;/h6,9H,2-5,8H2,1H3,(H,10,11);1H/t6-;/m0./s1

InChI key

AQELUQTVJOFFBN-RGMNGODLSA-N

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生化/生理作用

Nε-甲基-L-赖氨酸是一种赖氨酸类似物,对产黄青霉的生长和孢子形成以及菌丝体形成苄基青霉素具有抑制作用。

包装

无底玻璃瓶。内含物装在插入的融合锥内。

储存分类代码

11 - Combustible Solids

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable


历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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Matthew F Bush et al.
The journal of physical chemistry. A, 111(32), 7753-7760 (2007-07-20)
The gas-phase structures of protonated and alkali-metal-cationized lysine (Lys) and epsilon-N-methyllysine (Lys(Me)) are investigated using infrared multiple photon dissociation (IRMPD) spectroscopy utilizing light generated by a free electron laser, in conjunction with ab initio calculations. IRMPD spectra of Lys.Li(+) and
Methylated lysines and 3-methylhistidine in myosin: tissue and developmental differences.
G Huszar
Methods in enzymology, 106, 287-295 (1984-01-01)
C A Regenstreif et al.
Canadian journal of microbiology, 32(6), 522-524 (1986-06-01)
alpha-Methyl lysine was investigated as a potential inhibitor of lysine transport in Escherichia coli and Bacillus sphaericus. At equimolar concentrations, no inhibition was observed in either organism, but at 10X and 100X the lysine concentration, alpha-methyl lysine caused a 20-50%
Duy P Nguyen et al.
Journal of the American Chemical Society, 131(40), 14194-14195 (2009-09-24)
Lysine methylation is an important post-translational modification of histone proteins that defines epigenetic status and controls heterochromatin formation, X-chromosome inactivation, genome imprinting, DNA repair, and transcriptional regulation. Despite considerable efforts by chemical biologists to synthesize modified histones for use in
B Maras et al.
European journal of biochemistry, 203(1-2), 81-87 (1992-01-15)
The complete amino acid sequence of glutamate dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus has been determined. The sequence was reconstructed by automated sequence analysis of peptides obtained after cleavage by trypsin, cyanogen bromide, Staphylococcus aureus V8 protease and pepsin.

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