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Merck
CN

G7378

Sigma-Aldrich

甘氨酰胺 盐酸盐

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线性分子式:
NH2CH2CONH2 · HCl
化学文摘社编号:
分子量:
110.54
Beilstein:
3554199
EC 号:
MDL编号:
UNSPSC代码:
12352200
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pH值(酸碱度)

7.4-8.8

pKa (25 °C)

8.1

pKa (20 °C)

8.20

SMILES字符串

Cl.NCC(N)=O

InChI

1S/C2H6N2O.ClH/c3-1-2(4)5;/h1,3H2,(H2,4,5);1H

InChI key

WKNMKGVLOWGGOU-UHFFFAOYSA-N

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储存分类代码

13 - Non Combustible Solids

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

Eyeshields, Gloves, type N95 (US)

法规信息

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Hong Zhao et al.
Bioconjugate chemistry, 17(2), 341-351 (2006-03-16)
The utility of PEGylation for improving therapeutic protein pharmacology would be substantially expanded if the authentic protein drugs could be regenerated in vivo. Diminution of kinetic constants of both enzymes and protein ligands are commonly encountered following permanent bioconjugation with
Ajeet Singh et al.
Langmuir : the ACS journal of surfaces and colloids, 23(10), 5406-5411 (2007-04-14)
Conformational behaviors of urea and glycinamide have been investigated using the B3LYP functional with the 6-311+G* and 6-311+G** basis sets. Urea monomers have nonplanar minima at all the levels studied, even in the aqueous phase. In the case of glycinamide
Yong Sun et al.
The journal of physical chemistry. B, 109(12), 5919-5926 (2006-07-21)
For the purpose of investigating the tautomerism from glycinamide (G) to glycinamidic acid (G*) induced by proton transfer, we carried out a study of structural interconversion of the two tautomers and the relative stabilizing influences of water during the tautomerization
Samir Abdurahman et al.
Antimicrobial agents and chemotherapy, 52(10), 3737-3744 (2008-07-23)
Upon maturation of the human immunodeficiency virus type 1 (HIV-1) virion, proteolytic cleavage of the Gag precursor protein by the viral protease is followed by morphological changes of the capsid protein p24, which will ultimately transform the virus core from
Len Ito et al.
FEBS letters, 585(3), 555-560 (2011-01-18)
Glycine amide (GlyAd), a typically amidated amino acid, is a versatile additive that suppresses protein aggregation during refolding, heat treatment, and crystallization. In spite of its effectiveness, the exact mechanism by which GlyAd suppresses protein aggregation remains to be elucidated.

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