Purification and characterization of a novel phospholipase A2 from king cobra (Ophiophagus hannah) venom View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1995-08

AUTHORS

Jen-Yirng Chiou, Long-Sen Chang, Lyn-Nou Chen, Chun-Chang Chang

ABSTRACT

A novel phospholipase A2, designated as Oh-DE-2, was isolated from the venom ofOphiophagus hannah (king cobra) by successive chromatography on SP-Sephadex C-25, DE-52, and Q-Sepharose columns. Oh-DE-2 with pI 5.1 showed an apparent molecular weight of 14 kD as revealed by SDS-PAGE and gel filtration. The amino acid sequence was homologous with those of PLA2s from Elapidae venoms. Oh-DE-2 was effectively inactivated byp-bromophenacyl bromide, indicating that the conserved His-48 is essential for its enzymatic activity. However, modification of the conserved Trp-19 did not cause a precipitous drop in the enzymatic activity of Oh-DE-2 as observed with PLA2s fromNaja naja atra andBungarus multicinctus venoms. A quenching study showed that the microenvironment of Trp in Oh-DE-2 was inaccessible to acrylamide, iodide, or cesium, a finding which was different from those observed with PLA2s fromN. naja atra andB. multicinctus venoms. These results might suggest that, unlike other PLA2 enzymes, Trp-19 in Oh-DE-2 is not directly involved in its enzymatic mechanisms. More... »

PAGES

451-456

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf01888139

DOI

http://dx.doi.org/10.1007/bf01888139

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1031582671

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8593185


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