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首页> 外文期刊>Journal of biochemical and molecular toxicology >Purification and activity of two phospholipase enzymes from Naja nigricolis nigricolis reinhardt venom.
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Purification and activity of two phospholipase enzymes from Naja nigricolis nigricolis reinhardt venom.

机译：眼镜蛇（Naja nigricolis nigricolis reinhardt）毒液中两种磷脂酶的纯化和活性。

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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 &mgr;mol 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. Copyright 2003 Wiley Periodicals, Inc. J Biochem Mol Toxicol 17:53-58, 2003; Published online in Wiley InterScience(www.interscience.wiley.com). DOI 10.1002/jbt.10060
机译：从Naja nigricolis nigricolis Reinhardt的毒液中纯化了两种磷脂酶NN1和NN2，使其具有明显的同质性。 NN1在DEAE-纤维素柱上通过两步阴离子交换色谱法纯化，而NN2在Sephadex G-150上通过阴离子交换色谱法和凝胶过滤的组合纯化。酶NN1作为分子量为65 kDa的单体在丙烯酰胺凝胶上均匀移动，而NN2为71 kDa的二聚体。两种酶被清楚地分离。两种酶均水解L-α-磷脂酰胆碱，其对NN1的活性为345.5，对NN2的活性为727.8 mg·mol min（-1）mg（-1）。二聚体71-kDa酶比单体65-kDa酶具有更高的溶血和抗凝活性。显然，二聚酶比单体具有更明显的活性，因此毒性活性可能与磷脂的水解有关。版权所有2003 Wiley Periodicals，Inc. J Biochem Mol Toxicol 17：53-58，2003;在线发布于Wiley InterScience（www.interscience.wiley.com）。 DOI 10.1002 / jbt.10060

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