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Enzymatic properties of stingray Dasyatis pastinaca group V, IIA and IB phospholipases A2: A comparative study.
MedLine Citation:
PMID:  24120965     Owner:  NLM     Status:  Publisher    
In the present study, we have purified the group V phospholipase from the heart of cartilaginous fish stingray Dasyatis pastinaca and compared its biochemical properties with group IIA (sPLA2-IIA) and IB (sPLA2-IB) phospholipases previously purified from pancreas and intestine, respectively. Group V phospholipase (sPLA2-V) was purified to homogeneity by heat treatment, ammonium sulphate precipitation and RP-HPLC. The N-terminal sequence of the purified sPLA2-V exhibits a high degree of homology with those of mammal. The enzyme was found to be monomeric with a molecular mass estimation of 14kDa. The specific activity of the purified enzyme, measured at pH 8 and 37°C was 52U/mg. Like sPLA2-IB and sPLA2-IIA, the sPLA2-V is found to be stable between pH 3 and 11 after 30min of incubation. The purified sPLA2-V retained 65% of its activity after 10min of incubation at 70°C and it absolutely requires Ca(2+) for enzymatic activity. In addition it displayed high tolerance to organic solvents. Kinetic parameters Kmapp, kcat and the deduced catalytic efficiency (kcat/Kmapp) of the purified group-V, -IB and -IIA PLA2s were determined using phosphatidylethanolamine (PE), phosphatidylcholine (PC) or phosphatidylserine (PS) as substrate. The three enzymes hydrolyze the zwiterionic PE and PC substrates more efficiently than anionic PS substrate.
Abir Ben Bacha; Islem Abid; Habib Horchani; Hafedh Mejdoub
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-10-10
Journal Detail:
Title:  International journal of biological macromolecules     Volume:  -     ISSN:  1879-0003     ISO Abbreviation:  Int. J. Biol. Macromol.     Publication Date:  2013 Oct 
Date Detail:
Created Date:  2013-10-15     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7909578     Medline TA:  Int J Biol Macromol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2013. Published by Elsevier B.V.
Biochemistry Department, Science College, King Saud University, P.O. Box 22452, Riyadh 11495, Saudi Arabia; Laboratory of Plant Biotechnology Applied to Crop Improvement, Faculty of Science of Sfax, University of Sfax, Sfax 3038, Tunisia. Electronic address:
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