Solov'ev D A, Ugarova T P
Biokhimiia. 1993 Aug;58(8):1221-33.
Ancistron-H and Ancistron-B--two novel thrombin-like serine proteinases--have been purified 188- and 194-fold with a 95% recovery from the venoms of two Middle Asian subspecies of the pit viper--Agkistrodon halys halys and Agkistrodon halys Blomhoffii, using one-step affinity chromatography on agarose with an immobilized dye--Cibacron Blue F3GA (Blue-Sepharose 6B CL). The purified enzymes are one-chain glycoproteins with molecular masses of 34 and 29 kDa, pI of 6.6 and 6.3 and specific activities of 410 and 110 NIH units/mg protein, respectively. Their major amino acids are Gly, Val, Ser and Asp for Ancistron-H and Glu, Gly, Ser and Asp for Ancistron-B. During incubation with fibrinogen the enzymes cleave only the fibrinopeptide A from the A alpha-chain, leaving the B beta- and gamma-chains intact. Both enzymes hydrolyse arginine esters and thrombin-specific chromogenic peptide substrates, and display a weak caseinolytic activity but no fibrinolytic activity.
Ancistron-H和Ancistron-B——两种新型的类凝血酶丝氨酸蛋白酶——通过使用固定化染料Cibacron Blue F3GA（Blue-Sepharose 6B CL）的琼脂糖一步亲和层析法，从蝰蛇中亚两个亚种——极北蝰和岩栖蝰的毒液中纯化得到，纯化倍数分别为188倍和194倍，回收率达95%。纯化后的酶为单链糖蛋白，分子量分别为34 kDa和29 kDa，pI分别为6.6和6.3，比活性分别为410和110 NIH单位/毫克蛋白。Ancistron-H的主要氨基酸为甘氨酸、缬氨酸、丝氨酸和天冬氨酸，Ancistron-B的主要氨基酸为谷氨酸、甘氨酸、丝氨酸和天冬氨酸。在与纤维蛋白原孵育过程中，这些酶仅从Aα链上切割下纤维蛋白肽A，而使Bβ链和γ链保持完整。两种酶都能水解精氨酸酯和凝血酶特异性生色肽底物，并表现出较弱的酪蛋白水解活性，但无纤维蛋白溶解活性。
