Purification and characterization of two acidic phospholipase A2 enzymes from king cobra (Ophiophagus hannah) snake venom

1. 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...

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Main Authors: Nget-Hong, T., Saifuddin, M.N.
Format: Article
Language:en_US
Published: 2017
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spelling my.uniten.dspace-60532018-02-21T04:28:45Z Purification and characterization of two acidic phospholipase A2 enzymes from king cobra (Ophiophagus hannah) snake venom Nget-Hong, T. Saifuddin, M.N. 1. 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. 2017-12-08T08:12:28Z 2017-12-08T08:12:28Z 1990 Article 10.1016/0020-711X(90)90261-Z en_US Purification and characterization of two acidic phospholipase A2 enzymes from king cobra (Ophiophagus hannah) snake venom. International Journal of Biochemistry, 22(5), 481-487
institution Universiti Tenaga Nasional
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continent Asia
country Malaysia
content_provider Universiti Tenaga Nasional
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language en_US
description 1. 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.
format Article
author Nget-Hong, T.
Saifuddin, M.N.
spellingShingle Nget-Hong, T.
Saifuddin, M.N.
Purification and characterization of two acidic phospholipase A2 enzymes from king cobra (Ophiophagus hannah) snake venom
author_facet Nget-Hong, T.
Saifuddin, M.N.
author_sort Nget-Hong, T.
title Purification and characterization of two acidic phospholipase A2 enzymes from king cobra (Ophiophagus hannah) snake venom
title_short Purification and characterization of two acidic phospholipase A2 enzymes from king cobra (Ophiophagus hannah) snake venom
title_full Purification and characterization of two acidic phospholipase A2 enzymes from king cobra (Ophiophagus hannah) snake venom
title_fullStr Purification and characterization of two acidic phospholipase A2 enzymes from king cobra (Ophiophagus hannah) snake venom
title_full_unstemmed Purification and characterization of two acidic phospholipase A2 enzymes from king cobra (Ophiophagus hannah) snake venom
title_sort purification and characterization of two acidic phospholipase a2 enzymes from king cobra (ophiophagus hannah) snake venom
publishDate 2017
_version_ 1644493830293028864