Kynurenine aminotransferase/human hepatic C-S lyase: Preliminary structure-activity relationship studies

Blagbrough, Ian S., Buckberry, Lorraine D., Bycroft, Barrie W. and Shaw, P. Nicholas (1992) Kynurenine aminotransferase/human hepatic C-S lyase: Preliminary structure-activity relationship studies. Bioorganic and Medicinal Chemistry Letters, 2 10: 1219-1224. doi:10.1016/S0960-894X(00)80217-6


Author Blagbrough, Ian S.
Buckberry, Lorraine D.
Bycroft, Barrie W.
Shaw, P. Nicholas
Title Kynurenine aminotransferase/human hepatic C-S lyase: Preliminary structure-activity relationship studies
Journal name Bioorganic and Medicinal Chemistry Letters   Check publisher's open access policy
ISSN 0960-894X
1464-3405
Publication date 1992-10
Sub-type Article (original research)
DOI 10.1016/S0960-894X(00)80217-6
Volume 2
Issue 10
Start page 1219
End page 1224
Total pages 6
Place of publication Oxford, United Kingdom
Publisher Pergamon
Language eng
Abstract Partially purified human hepatic cytosolic and mitochondrial fractions have been investigated for evidence of C-S lyase (CSL) activity. CSL activity has been characterized with synthetic aliphatic and aromatic L-cysteine conjugates. Preliminary structure-activity relationship studies have shown that aliphatic and aromatic L-cysteine conjugates are substrates.
Keyword Conjugate beta-lyase
Cysteine
Nephrotoxicity
Metabolites
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Pharmacy Publications
 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 1 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 1 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Mon, 20 Dec 2010, 14:04:29 EST