PMID: 8593185Aug 1, 1995Paper

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

Journal of Protein Chemistry
J Y ChiouC C Chang

Abstract

A novel phospholipase A2, designated as Oh-DE-2, was isolated from the venom of Ophiophagus 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 by p-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 from Naja naja atra and Bungarus 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 from N. naja atra and B. 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.

References

Apr 15, 1992·Biochemical and Biophysical Research Communications·K TomooY Samejima
Dec 14, 1990·Science·D L ScottP B Sigler
Jan 1, 1981·Toxicon : Official Journal of the International Society on Toxinology·C C YangT P Sun
Jan 1, 1981·Journal of Biochemistry·K KondoK Narita
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Mar 15, 1994·Biochemical and Biophysical Research Communications·F M PanS H Chiou
Dec 28, 1971·Biochimica Et Biophysica Acta·C C ChangK Hayashi

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Citations

Aug 2, 2011·Journal of Proteomics·Paula H C CiscottoAdriano M C Pimenta
Aug 11, 2006·Toxicon : Official Journal of the International Society on Toxinology·Long-Sen ChangHsien-Bin Huang
Jul 7, 2019·The Protein Journal·Pakamas WongtayAphichart Karnchanatat

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