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从巨蝮(Lachesis muta)毒液(蛇亚目:蝰蛇科)中分离出的一种凝血蛋白酶的纯化及性质

Purification and properties of a coagulant proteinase isolated from bushmaster (Lachesis muta) venom (Serpentes: Viperidae).

作者信息

Aragón-Ortiz F

机构信息

Dpto. de Bioquímica, Escuela de Medicina, Universidad de Costa Rica.

出版信息

Rev Biol Trop. 1986 Jun;34(1):55-8.

PMID:3313549
Abstract

The venom of Lachesis muta is a rich source of a thrombin-like enzyme. Its coagulant proteinase was purified by DEAE -Sephadex A -50 followed by agmatine CH -Sepharose and gel filtration on Sephadex G-100. On polyacrylamide gel electrophoresis at pH 8.4 a single band was observed. Its molecular weight by gel filtration was 49,000. The coagulant and esterolytic activities toward human fibrinogen and Tame of the inudasa were 662 NIH units/mg of protein and 4.37 delta OD225/min x 10(-3)/micrograms/ml, respectively. These values represent 23 and 5.7 fold increase over the crude venom. The enzyme mudasa, was evaluated with serum from human patients at Hospital Nacional de Niños Dr. Carlos Sáenz Herrera and found to be a valuable reagent for the quantification of fibrinogen on heparinized plasma.

摘要

巨蝮蛇毒是凝血酶样酶的丰富来源。其凝血蛋白酶通过DEAE - 葡聚糖A - 50进行纯化,随后用胍丁胺CH - 葡聚糖凝胶进行纯化,并在葡聚糖凝胶G - 100上进行凝胶过滤。在pH 8.4的聚丙烯酰胺凝胶电泳中观察到一条单一的条带。通过凝胶过滤测得其分子量为49,000。对人纤维蛋白原的凝血活性和酯解活性分别为662 NIH单位/毫克蛋白质和4.37 ΔOD225/分钟×10⁻³/微克/毫升。这些值分别比粗毒液增加了23倍和5.7倍。该酶被卡洛斯·萨恩斯·埃雷拉国立儿童医院的人类患者血清评估,发现它是用于定量肝素化血浆中纤维蛋白原的一种有价值的试剂。

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