蛇毒丝氨酸蛋白酶多样性──底物专一性免疫化学及序列比较研究  被引量:2

SNAKE VENOM SERINE PROTEASE DIVERSITY──SUBSTRATE SPECTIFICITY IMMUNO-CHEMISTRY AND SEQUENCE COMPARISON STUDIES

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作  者:张沄 熊郁良[1] 王婉瑜[1] 李文辉[1] 朱绍文[1] 

机构地区:[1]中国科学院昆明动物研究所

出  处:《Zoological Research》1994年第3期73-80,共8页动物学研究(英文)

摘  要:本文报道烙铁头(Trimeresurusmucrosquamatus)蛇毒纤维蛋白原溶酶(TMVFg),眼镜王蛇(Ophiophagushannah)蛇毒纤维蛋白原溶酶(ohS1),竹叶青(Trimeresurusstejnegeri)蛇毒专一纤溶酶原激活剂(sv-pA)对5种小分子多肽底物的底物专一性,及这些蛇毒丝氨酸蛋白酶对各种凝血因子(第X因子、凝血酶原、纤溶酶原、蛋白C)的作用,并和其它蛇毒丝氨酸蛋白酶如矛头蝮(Bothropsatrox)蛇毒凝血酶样酶(Batroxobin)、铜头蝮(Agkistrodoncontortrixcontortrix)蛇毒蛋白C激活剂ACC-C、蝰蛇(Viperarusselli)毒第Ⅴ因子激活剂RVV-V进行比较研究。通过酶标偶联免疫反应研究了抗sv-PA抗体与各种丝氨酸蛋白酶的免疫交叉反应,并对蛇毒丝氨酸蛋白酶及相应功能的哺乳动物蛋白酶进行了序列比较分析。从底物专一性多样性及已知序列结构分化上对这一类蛇毒丝氨酸蛋白酶的结构与功能进行了探讨和研究。The substrate specificities of TMVFg (a fibrinogenase from Trimeresurus mucrosquamatus venom), OhS1 (a fibrinogenase from Ophiophagus hannah venom) and sv-PA (a speciflc plasminogen activator from Trimeresurus stefnegeri venom) on five chromogenic substrates were studied. Further, We studied the effects of these venom serine proteases on purified blood coagulation factors, like factor X, prothrombin, plasminogen and protein C.The comparison studies were dealed with other venom serine proteases,like Bothrops atrox venom thrombin-like enzyme (Batroxobin),Agkistrodon contortrix contortrix venom protein C activator (ACC-C) and Vipera russelli venom factor V activator (RVV-V). and also with trypsin, thrombin, urokinase.Immunochemical study by ELISA proved that anti-sv-PA antibodies cross-reacted with other venom serine proteases but did not cross react with thrombin, urokinase and t-PA.We also compared the sequences of these serine proteases. Based on the results of substrate specificity, immuno-chemistry and sequence comparasion, the paper give the discussion on the structure function relationship of these serine proteases.

关 键 词:蛇毒 蛋白酶 序列  免疫化学 

分 类 号:Q959.620.6[生物学—动物学]

 

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