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  3. COE Scholarly Publication
Please use this identifier to cite or link to this item: http://dspace.uniten.edu.my/jspui/handle/123456789/6056
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dc.contributor.authorTan, N.H.en_US
dc.contributor.authorSaifuddin, M.N.en_US
dc.date.accessioned2017-12-08T08:12:29Z-
dc.date.available2017-12-08T08:12:29Z-
dc.date.issued2000-
dc.identifier.urihttps://pure.uniten.edu.my/en/publications/isolation-and-characterization-of-an-unusual-form-of-l-amino-acid-
dc.description.abstractThe 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.isoenen_US
dc.relation.ispartofIsolation and characterization of an unusual form of L-amino acid oxidase from King cobra (Ophiophagus hannah) venom. Biochemistry International, 19(4), 937-94en_US
dc.titleIsolation and characterization of an unusual form of L-amino acid oxidase from King cobra (Ophiophagus hannah) venomen_US
dc.typeArticleen_US
item.grantfulltextnone-
item.fulltextNo Fulltext-
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