Isolation and characterization of an unusual form of L-amino acid oxidase from King cobra (Ophiophagus hannah) venom

Please use this identifier to cite or link to this item: http://dspace.uniten.edu.my/jspui/handle/123456789/6056

DC Field	Value	Language
dc.contributor.author	Tan, N.H.	en_US
dc.contributor.author	Saifuddin, M.N.	en_US
dc.date.accessioned	2017-12-08T08:12:29Z	-
dc.date.available	2017-12-08T08:12:29Z	-
dc.date.issued	2000	-
dc.identifier.uri	https://pure.uniten.edu.my/en/publications/isolation-and-characterization-of-an-unusual-form-of-l-amino-acid	-
dc.description.abstract	The L-amino acid oxidase (EC 1.4.3.2) from King cobra (Ophiophagus hannah) venom was purified to electrophoretic homogeneity. The molecular weight of the enzyme was determined to be 140000 when examined by gel filtration and 68000 by SDS-polyacrylamide gel electrophoresis. The enzyme had an isoelectric point of 4.5 and an intravenous LD50 of 5 μg/g in mice. It is a glycoprotein and contains two moles of FAD per mole of enzyme. The enzyme exhibited unusual thermal stability and unlike most other venom L-amino acid oxidases, it was stable in alkaline solution and was not inactivated by freezing.	en_US
dc.language.iso	en	en_US
dc.relation.ispartof	Isolation and characterization of an unusual form of L-amino acid oxidase from King cobra (Ophiophagus hannah) venom. Biochemistry International, 19(4), 937-94	en_US
dc.title	Isolation and characterization of an unusual form of L-amino acid oxidase from King cobra (Ophiophagus hannah) venom	en_US
dc.type	Article	en_US
item.fulltext	No Fulltext	-
item.grantfulltext	none	-
Appears in Collections:	COE Scholarly Publication

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