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

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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.

Original languageEnglish
Pages (from-to)937-944
Number of pages8
JournalBiochemistry International
Volume19
Issue number4
Publication statusPublished - 1989

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L-Amino Acid Oxidase
Elapidae
Venoms
Enzymes
Flavin-Adenine Dinucleotide
Lethal Dose 50
Isoelectric Point
Electrophoresis
Freezing
Gel Chromatography
Polyacrylamide Gel Electrophoresis
Glycoproteins
Thermodynamic stability
Hot Temperature
Molecular Weight
Gels
Molecular weight

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

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AU - Tan, N. H.

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N2 - 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.

AB - 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.

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