Kynurenine aminotransferase activity in human liver: identity with human hepatic C-S lyase activity and a physiological role for this enzyme

Buckberry, Lorraine D., Blagbrough, Ian S., Bycroft, Barrie W. and Shaw, P. Nicholas (1992) Kynurenine aminotransferase activity in human liver: identity with human hepatic C-S lyase activity and a physiological role for this enzyme. Toxicology Letters, 60 3: 241-246. doi:10.1016/0378-4274(92)90281-N


Author Buckberry, Lorraine D.
Blagbrough, Ian S.
Bycroft, Barrie W.
Shaw, P. Nicholas
Title Kynurenine aminotransferase activity in human liver: identity with human hepatic C-S lyase activity and a physiological role for this enzyme
Journal name Toxicology Letters   Check publisher's open access policy
ISSN 0378-4274
1879-3169
Publication date 1992-05-01
Sub-type Article (original research)
DOI 10.1016/0378-4274(92)90281-N
Volume 60
Issue 3
Start page 241
End page 246
Total pages 6
Place of publication Shannon, Co. Clare Ireland
Publisher Elsevier
Language eng
Abstract The C-S lyase enzymes are responsible for the generation of mutagenic and cytotoxic metabolites via aberrant drug-metabolising pathways in mammalian tissues. We have examined human hepatic cytosolic, mitochondrial and microsomal fractions for evidence of C-S lyase activity. The cytosolic enzyme was purified using fast protein liquid chromatography over FFQ Sepharose, Mono P and Superose 12. An homogeneous protein (monitored by SDS-PAGE) was obtained following purification, and an 11-fold increase in C-S lyase specific activity was observed. The molecular weight of the enzyme was found to be 37 kDa in denaturing conditions, 82.3 kDa in non-denaturing conditions, and the C-S lyase activity was shown to co-purify with kynurenine aminotransferase activity when the transaminase activity of the enzyme was examined with kynurenine as the substrate.
Keyword Cysteine Conjugate Beta-lyase
C-s Lyase
Kynurenine Aminotransferase
Human Hepatic Tissue
S-(e-1,2-dichlorovinyl)-l-cysteine
Dcvc
Conjugate Beta-lyase
Cysteine
Transaminase
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 17 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 14 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Tue, 21 Dec 2010, 00:04:59 EST