product name
L -胱氨酸, ≥99.7% (TLC)
质量水平
检测方案
≥99.7% (TLC)
形式
powder or crystals
旋光性
[α]20/D −219±5°, c = 1% in 1 M HCl
灼烧残渣
≤0.1% (as SO4)
缺失
≤0.1% loss on drying
颜色
white
mp
>240 °C (dec.) (lit.)
溶解性
1 M HCl: 0.5 g/10 mL, clear, colorless
痕量阴离子
chloride (Cl-): ≤500 mg/kg
sulfate (SO42-): ≤100 mg/kg
痕量阳离子
Ca: ≤50 mg/kg
Cd: ≤5 mg/kg
Co: ≤5 mg/kg
Cr: ≤5 mg/kg
Cu: ≤6 mg/kg
Fe: ≤10 mg/kg
K: ≤50 mg/kg
Mg: ≤5 mg/kg
Mn: ≤5 mg/kg
Na: ≤150 mg/kg
Ni: ≤5 mg/kg
Pb: ≤5 mg/kg
Zn: ≤5 mg/kg
应用
peptide synthesis
SMILES字符串
N[C@@H](CSSC[C@H](N)C(O)=O)C(O)=O
InChI
1S/C6H12N2O4S2/c7-3(5(9)10)1-13-14-2-4(8)6(11)12/h3-4H,1-2,7-8H2,(H,9,10)(H,11,12)/t3-,4-/m0/s1
InChI key
LEVWYRKDKASIDU-IMJSIDKUSA-N
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应用
L-胱氨酸已被用于制备原液，该原液又通过光谱荧光流动注射法用于测定药物制剂以及尿液样品中的L-半胱氨酸和L-胱氨酸。
生化/生理作用
胱氨酸是合成保护细胞免受氧化应激的谷胱甘肽所必需的。一种特殊的 x (c)-半胱氨酸/谷氨酸反向转运蛋白可介导细胞摄取半胱氨酸以交换谷氨酸。半胱氨酸摄取抑制诱导神经元细胞毒性。
其他说明
用于 N,N′-二苯甲酰基-L-胱氨酸的制备，酮不对称还原的高效辅助剂
WGK
WGK 1
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
T H Murphy et al.
Neuron, 2(6), 1547-1558 (1989-06-01)
Glutamate binds to both excitatory neurotransmitter binding sites and a Cl(-)-dependent, quisqualate- and cystine-inhibited transport site on brain neurons. The neuroblastoma-primary retina hybrid cells (N18-RE-105) are susceptible to glutamate-induced cytotoxicity. The Cl(-)-dependent transport site to which glutamate and quisqualate (but
Journal of the Chemical Society. Chemical Communications, 801-801 (1987)
T Pérez-Ruiz et al.
The Analyst, 117(6), 1025-1028 (1992-06-01)
A flow injection configuration is proposed for the determination of L-cysteine and L-cystine individually and for mixtures of both analytes. The procedure is based on the rapid oxidation of L-cysteine by thallium(III) with concomitant formation of fluorescent thallium(I). The inclusion
K. Soai et al.
Journal of the Chemical Society. Chemical Communications, 413-413 (1984)
Philip J Hogg
Nature reviews. Cancer, 13(6), 425-431 (2013-05-11)
Protein action in nature is generally controlled by the amount of protein produced and by chemical modification of the protein, and both are often perturbed in cancer. The amino acid side chains and the peptide and disulphide bonds that bind
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