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Biotechnology & Biotechnological Equipment 27 (5), 4181 - 4185 (2013)
http://dx.doi.org/10.5504/BBEQ.2013.0072

EDUCATION & BASIC SCIENCE

EFFECT OF SOME DIVALENT METAL IONS ON ENZYMАTIC ACTIVITY OF SECRETED PHOSPHOLIPASE A2 (sPLA2) ISOLATED FROM BULGARIAN VIPERA AMMODYTES MERIDIONALIS

Vasil Atanasov1, 2, Silviya Stoykova1, 2, Hristo Kolev3, Mariana Mitewa1, Svetla Petrova4, Ivayla Pantcheva1

  1. Sofia University, Faculty of Chemistry and Pharmacy, Sofia, Bulgaria
  2. Military Medical Academy, Emergency Toxicology Clinic, Sofia, Bulgaria
  3. University, Faculty of Chemistry and Pharmacy, Sofia, Bulgaria
  4. Sofia University, Faculty of Biology, Sofia, Bulgaria

Correspondence to: Vasil Atanasov E-mail: VAtanasov@chem.uni-sofia.bg; Ivayla Pantcheva E-mail: IPancheva@chem.uni-sofia.bg

Published 17 October 2013

Abstract

The effect of Ca2+ and some divalent metal ions related to it (Mg, Sr, Ba, Cd) on the hydrolysis of natural and artificial substrates catalyzed by vipoxin secreted phospholipase A2 subunit (sPLA2) was evaluated. The results showed that the hydrolysis of natural glycerophospholipids proceeds at a highest rate when the enzyme is activated by calcium ions. The catalytic activity of sPLA2 decreased in the presence of other metal ions possibly due to their lower coordination ability to the head group of lipids. Oppositely, the hydrolysis of artificial substrates was facilitated by metal ions with ionic radii larger than Ca2+, such as Sr2+ and Ba2+,suggesting that not only the interaction with metal cations, but also the origin of the head group should be considered. The fluorescence assay revealed that conformational changes occur during the coordination of metal ions into the catalytic site of sPLA2 prior to subsequent hydrolysis. It could be concluded that the rate-limiting step in the catalytic cycle (e.g. the chemical interaction) is not completely adequate to evaluate all factors affecting the hydrolytic activity of vipoxin sPLA2.

Keywords
vipoxin, sPLA2, divalent metal ions

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