Purification and activity of two phospholipase enzymes from Naja nigricolis nigricolis Reinhardt venom

被引:2
作者
Abubakar, MS [1 ]
Nok, AJ
Abdurahman, EM
Haruna, AK
Shok, M
机构
[1] Ahmadu Bello Univ, Fac Pharmaceut Sci, Dept Pharmacognosy & Drug Dev, Zaria, Nigeria
[2] Ahmadu Bello Univ, Fac Sci, Dept Biochem, Zaria, Nigeria
[3] Ahmadu Bello Univ, Fac Pharmaceut Sci, Dept Pharmaceut & Med Chem, Zaria, Nigeria
关键词
venom; phospholipase; Naja nigricolis nigricolis;
D O I
10.1002/jbt.10060
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Two phospholipase enzymes NN1 and NN2 were purified from the venom of Naja nigricolis nigricolis Reinhardt to apparent homogeneity. NN1 was purified by a two-step anion-exchange chromatography on DEAE-cellulose column while NN2 was purified by a combination of anion-exchange chromatography and gel filteration on Sephadex G-150. The enzyme NN1 moved homogenously on acrylamide gel as a monomer with a molecular weight of 65 kDa while NN2 was a dimer of 71 kDa. Both enzymes were clearly separated. Both enzymes hydrolyzed L-alpha-phosphatidyl choline with activities of 345.5 for NN1 and 727.8 mumol min(-1) mg(-1) for NN2. The dimeric 71-kDa enzyme has a higher haemolytic and anticoagulant activity than the monomeric 65-kDa enzyme. It is apparent that the dimeric enzyme has a more pronounced activity than the monomer has, thus toxic activity may be related to the hydrolysis of phospholipids. (C) 2003 Wiley Periodicals, Inc.
引用
收藏
页码:53 / 58
页数:6
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