Document Detail


Purification and properties of the L-amino acid oxidase from monocellate cobra (Naja naja kaouthia) venom.
MedLine Citation:
PMID:  1612186     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
1. The L-amino acid oxidase of the monocellate cobra (Naja naja kaouthia) venom was purified to electrophoretic homogeneity. The molecular weight of the enzyme was 112,200 as determined by Sephadex G-200 gel filtration chromatography, and 57,400 as determined by SDS-polyacrylamide gel electrophoresis. 2. The enzyme had an isoelectric point of 8.12 and a pH optimum of 8.5. It showed remarkable thermal stability, and, unlike many venom L-amino acid oxidase, was also stable in alkaline medium. The enzyme was partially inactivated by freezing. 3. The enzyme was very active against L-phenylalanine and L-tyrosine, moderately active against L-tryptophan, L-methionine, L-leucine, L-norleucine, L-arginine and L-norvaline. Other L-amino acids were oxidized slowly or not oxidized. 4. Kinetic studies suggest the presence of a side-chain binding site in the enzyme, and that the binding site comprises of at least four hydrophobic subsites.
Authors:
N H Tan; S Swaminathan
Related Documents :
2553736 - The brown alga ascophyllum nodosum contains two different vanadium bromoperoxidases.
25184516 - Trpb2 enzymes are o-phospho-l-serine dependent tryptophan synthases.
1729236 - Purification of a nocardicin a-sensitive ld-carboxypeptidase from escherichia coli by a...
3106336 - Purification and properties of the hydroxylase component of methane monooxygenase.
6381476 - N-benzyloxycarbonyl-valyl-prolinal, a potent inhibitor of post-proline cleaving enzyme.
18280576 - Renewable enzyme reactors based on beds of artificial gel antibodies.
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The International journal of biochemistry     Volume:  24     ISSN:  0020-711X     ISO Abbreviation:  Int. J. Biochem.     Publication Date:  1992 Jun 
Date Detail:
Created Date:  1992-07-28     Completed Date:  1992-07-28     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0250365     Medline TA:  Int J Biochem     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  967-73     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, University of Malaya, Kuala Lumpur, Malaysia.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Amino Acid Oxidoreductases / isolation & purification,  metabolism*
Amino Acids / metabolism
Chromatography, Gel
Chromatography, Ion Exchange
Cobra Venoms / enzymology*
Hydrogen-Ion Concentration
Kinetics
L-Amino Acid Oxidase
Oxidation-Reduction
Substrate Specificity
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Cobra Venoms; EC 1.4.-/Amino Acid Oxidoreductases; EC 1.4.3.2/L-Amino Acid Oxidase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Intralobular localization of different cytochrome P-450 form dependent monooxygenase activities in t...
Next Document:  Amino acid composition and immunochemical properties of AcPase III and AcPase IV representing glycof...