Please use this identifier to cite or link to this item: http://dspace.uniten.edu.my/jspui/handle/123456789/6053
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dc.contributor.authorNget-Hong, T.en_US
dc.contributor.authorSaifuddin, M.N.en_US
dc.date.accessioned2017-12-08T08:12:28Z-
dc.date.available2017-12-08T08:12:28Z-
dc.date.issued1990-
dc.description.abstract1. 1. The two major phospholipase A2 enzymes (OHPLA-DE1 and OHPLA-DE2) of king cobra (Ophiophagus hannah) venom have been purified to electrophoretic homogeneity. 2. 2. The isoelectric points of OHPLA-DE1 and OHPLA-DE2 were 3.81 and 3.89, respectively and the Mws were 14,000 and 15,000, respectively, as estimated by Sephadex G-75 gel filtration chromatography; and 14,000 as estimated by SDS-PAGE. 3. 3. The enzymes were not lethal to mice at a dosage of 10 μg/g body wt by i.v. route. Both phospholipase A2 enzymes, however, exhibited moderate edema-inducing and anti-coagulant activities. 4. 4. Bromophenacylation of the enzymes reduced the enzymatic activity drastically but did not affect the edema-inducing activity of the enzymes. © 1990.en_US
dc.language.isoen_USen_US
dc.relation.ispartofPurification and characterization of two acidic phospholipase A2 enzymes from king cobra (Ophiophagus hannah) snake venom. International Journal of Biochemistry, 22(5), 481-487en_US
dc.titlePurification and characterization of two acidic phospholipase A2 enzymes from king cobra (Ophiophagus hannah) snake venomen_US
dc.typeArticleen_US
dc.identifier.doi10.1016/0020-711X(90)90261-Z-
item.grantfulltextnone-
item.fulltextNo Fulltext-
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