质量水平
检测方案
≥99.0% (NT)
形式
solid
反应适用性
reaction type: solution phase peptide synthesis
mp
~250 °C (dec.)
应用
peptide synthesis
SMILES字符串
CS(=O)(=O)CCC(N)C(O)=O
InChI
1S/C5H11NO4S/c1-11(9,10)3-2-4(6)5(7)8/h4H,2-3,6H2,1H3,(H,7,8)
InChI key
UCUNFLYVYCGDHP-UHFFFAOYSA-N
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相关类别
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
Asian-Australasian journal of animal sciences, 30(8), 1150-1159 (2017-02-12)
This study was conducted to evaluate various wheat supplementation levels on growth performance, blood profiles, nutrient digestibility, and pork quality in growing-finishing pigs. A total of 120 growing pigs ([Yorkshire×Landrace]×Duroc), with an average 27.75± 1.319 kg body weight, were used
The British journal of nutrition, 46(1), 77-86 (1981-07-01)
1. The relative potencies of three lysine, one tryptophan and six methionine analogues to their corresponding l-amino acids were determined. 2. Male poults, 9 d of age, were used in five 14 d experiments. Experimental diets were formed by adding
Protein science : a publication of the Protein Society, 13(11), 2979-2991 (2004-10-23)
Glutamate synthase (GltS) is a complex iron-sulfur flavoprotein that catalyzes the reductive transfer of L-glutamine amide group to the C2 carbon of 2-oxoglutarate yielding two molecules of L-glutamate. Molecular dynamics calculations in explicit solvent were carried out to gain insight
Structure (London, England : 1993), 8(12), 1299-1308 (2001-02-24)
The complex iron-sulfur flavoprotein glutamate synthase catalyses the reductive synthesis of L-glutamate from 2-oxoglutarate and L-glutamine, a reaction in the plant and bacterial pathway for ammonia assimilation. The enzyme functions through three distinct active centers carrying out L-glutamine hydrolysis, conversion
Journal of general microbiology, 133(7), 1667-1674 (1987-07-01)
A glycine-resistant Neurospora crassa mutant (am-132;glyr), derived from the am-132 mutant, was isolated and characterized. [am-132 itself has a deletion in the structural gene for NADP-dependent glutamate dehydrogenase (GDH).] This new mutation also conferred resistance to serine and methionine sulphoximine
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