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核心技术专利：CN118964589B侵权必究

核心技术专利：CN118964589B侵权必究

Nikai T, Imai K, Nagasaka M, Sugihara H

Department of Microbiology, Faculty of Pharmacy, Meijo University, Nagoya, Japan.

Int J Biochem. 1988;20(11):1239-45. doi: 10.1016/0020-711x(88)90226-1.

A kallikrein-like enzyme was isolated from Agkistrodon p. piscivorus venom by Sephadex G-100, DEAE-Sephacel and S-Sepharose column chromatographies. 2. A kallikrein-like enzyme was shown to be homogeneous as demonstrated by a single band on acrylamide gel electrophoresis, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunodiffusion. 3. Its molecular weight is approx. 29,000 with an isoelectric point of 7.8. 4. A kallikrein-like enzyme is able to cleave a kininogen analog to release bradykinin, and the B beta chain of fibrinogen. These proteolytic and tosyl-L-arginine methyl ester hydrolytic activities were inhibited by diisopropyl fluorophosphate, suggesting that the serine hydroxyl group is involved in enzymatic activities.

通过葡聚糖凝胶G - 100、二乙氨基乙基葡聚糖凝胶（DEAE - Sephacel）和S - 琼脂糖凝胶柱色谱法从食鱼蝮蛇毒中分离出一种类激肽释放酶。2. 经丙烯酰胺凝胶电泳、十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳和免疫扩散显示，该类激肽释放酶呈均一性，表现为单一条带。3. 其分子量约为29,000，等电点为7.8。4. 该类激肽释放酶能够裂解激肽原类似物以释放缓激肽，以及纤维蛋白原的Bβ链。这些蛋白水解活性和甲苯磺酰 - L - 精氨酸甲酯水解活性被二异丙基氟磷酸抑制，表明丝氨酸羟基参与了酶活性。

Nikai T, Imai K, Nagasaka M, Sugihara H

Department of Microbiology, Faculty of Pharmacy, Meijo University, Nagoya, Japan.

Int J Biochem. 1988;20(11):1239-45. doi: 10.1016/0020-711x(88)90226-1.

A kallikrein-like enzyme was isolated from Agkistrodon p. piscivorus venom by Sephadex G-100, DEAE-Sephacel and S-Sepharose column chromatographies. 2. A kallikrein-like enzyme was shown to be homogeneous as demonstrated by a single band on acrylamide gel electrophoresis, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunodiffusion. 3. Its molecular weight is approx. 29,000 with an isoelectric point of 7.8. 4. A kallikrein-like enzyme is able to cleave a kininogen analog to release bradykinin, and the B beta chain of fibrinogen. These proteolytic and tosyl-L-arginine methyl ester hydrolytic activities were inhibited by diisopropyl fluorophosphate, suggesting that the serine hydroxyl group is involved in enzymatic activities.

通过葡聚糖凝胶G - 100、二乙氨基乙基葡聚糖凝胶（DEAE - Sephacel）和S - 琼脂糖凝胶柱色谱法从食鱼蝮蛇毒中分离出一种类激肽释放酶。2. 经丙烯酰胺凝胶电泳、十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳和免疫扩散显示，该类激肽释放酶呈均一性，表现为单一条带。3. 其分子量约为29,000，等电点为7.8。4. 该类激肽释放酶能够裂解激肽原类似物以释放缓激肽，以及纤维蛋白原的Bβ链。这些蛋白水解活性和甲苯磺酰 - L - 精氨酸甲酯水解活性被二异丙基氟磷酸抑制，表明丝氨酸羟基参与了酶活性。