来自食鱼蝮蛇毒液的β-纤维蛋白原酶。
Beta-fibrinogenase from the venom of Agkistrodon p. piscivorus.
作者信息
Nikai T, Katano E, Komori Y, Sugihara H
机构信息
Department of Microbiology, Faculty of Pharmacy, Meijo University, Nagoya, Japan.
出版信息
Comp Biochem Physiol B. 1988;89(3):509-15. doi: 10.1016/0305-0491(88)90166-6.
PMID:3359757
Abstract
- Beta-fibrinogenase was isolated from the venom of Agkistrodon p. piscivorus by column chromatography on Sephadex G-100, DEAE-Sephacel and by chromatofocusing, with a yield of 2.5 mg of purified enzyme from 1 g of crude venom. 2. The enzyme was homogeneous by SDS and non-SDS disc electrophoresis on polyacrylamide gel at pH 8.3. 3. Beta-fibrinogenase is a glycoprotein possessing both TAME hydrolase and kinin-releasing activities. 4. A mol. wt of approximately 33,500 and an isoelectric point 4.5 was determined. 5. The enzyme is stable to heat treatment and to a pH range of 2-10. 6. Beta-fibrinogenase activity is inactivated by DFP, suggesting that serine is involved in the enzymatic activity. 7. The Michaelis constant (Km) of this enzyme for TAME and inhibition constant (Ki) for DFP were found to be 7.04 X 10(-3) and 4.13 X 10(-3) M, respectively.
摘要
- 通过在葡聚糖凝胶G - 100、二乙氨基乙基葡聚糖凝胶（DEAE - Sephacel）上进行柱色谱以及聚焦层析，从食鱼蝮蛇毒中分离出β - 纤维蛋白原酶，从1克粗毒中可获得2.5毫克纯化酶。2. 在pH 8.3的聚丙烯酰胺凝胶上进行SDS和非SDS圆盘电泳时，该酶呈现均一性。3. β - 纤维蛋白原酶是一种糖蛋白，兼具对甲苯磺酰-L-精氨酸甲酯（TAME）水解酶和激肽释放活性。4. 测定其分子量约为33,500，等电点为4.5。5. 该酶对热处理以及pH值在2至10的范围稳定。6. β - 纤维蛋白原酶活性被二异丙基氟磷酸（DFP）灭活，表明丝氨酸参与酶活性。7. 发现该酶对TAME的米氏常数（Km）和对DFP的抑制常数（Ki）分别为7.04×10⁻³和4.13×10⁻³ M。
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