Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Editor

Personal info

View

About

Terms

Javascript disabled

Please enable Javascript support in your browser to use this application.

Instructions on how to enable JavaScript on different browsers can be found here: http://www.google.com/support/bin/answer.py?answer=23852.

[edit this page]

Chemical Compound Review:

AG-F-77715 2-amino-3-benzylsulfanyl-N- (4...

Synonyms: NSC-334320, AC1Q5MEW, CTK4J5600, NSC334320, AR-1L4013, ...

Murata, K. et al., Roy, A.C. et al., Hrabak, R. et al., Small, C.W. et al.

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of s-Benzyl-L-cysteine-p-nitroanilide

An enzyme that catalyzes hydrolysis of S-benzyl-L-cysteine-p-nitroanilide was purified from E. coli B [1].

High impact information on s-Benzyl-L-cysteine-p-nitroanilide

L-leucine and its analogue: specific inhibitors for S-benzyl-L-cysteine-p-nitroanilide-hydrolyzing enzyme in Escherichia coli B [1].
Cystine aminopeptidase (CAP) activity in tissues and in plasma from pregnant cows was measured at various stages of gestation by using the substrate S-benzyl-L-cysteine-4-nitroanilide [2].
A rapid and specific method for the determination of oxytocinase (cystine aminopeptidase) activity using continuous flow analysis and S-benzyl-L-cysteine-p-nitroanilide as substrate [3].

Associations of s-Benzyl-L-cysteine-p-nitroanilide with other chemical compounds

Oxytocinase (EC 3.4.11.3) activity was measured in uterine homogenates from pregnant and non-pregnant women using S-benzyl-L-cysteine-p-nitroanilide (BCN) and L-leucine-p-nitroanilide (LN) separately as substrates [4].

References

L-leucine and its analogue: specific inhibitors for S-benzyl-L-cysteine-p-nitroanilide-hydrolyzing enzyme in Escherichia coli B. Murata, K., Iba, Y., Inoue, Y., Kimura, A. Biochem. Biophys. Res. Commun. (1988) [Pubmed]
Cystine aminopeptidase (oxytocinase) activity in plasma and tissues of normal and infected pregnant cattle. Hrabak, R., Baetz, A.L., Cysewski, S.J. Am. J. Vet. Res. (1976) [Pubmed]
A rapid and specific method for the determination of oxytocinase (cystine aminopeptidase) activity using continuous flow analysis and S-benzyl-L-cysteine-p-nitroanilide as substrate. Small, C.W., Watkins, W.B. Clin. Biochem. (1975) [Pubmed]
Multimolecular forms of oxytocinase activity in the human uterus and their inhibition by prostaglandins and cyclic GMP. Roy, A.C., Yeang, M., Ho, L.M., Kottegoda, S.R., Ratnam, S.S. Prostaglandins, leukotrienes, and medicine. (1985) [Pubmed]

Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenes Open Access Licence Privacy Policy Terms of Use apsburg

The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.