用羰基二咪唑活化琼脂糖固定化蚯蚓纤溶酶III-1。

Immobilized earthworm fibrinolytic enzyme III-1 with carbonyldiimidazole activated-agarose.

作者信息

Wu Xue-Qin, Wu Cen, He Rong-qiao

机构信息

Lab of Visual Information Processing, Academic Center of Brain and cognition, Institute of Biophysics, The Chinese Academy of Sciences, 15 Da Tun Rd, Beijing 100101, China.

出版信息

Protein Pept Lett. 2002 Feb;9(1):75-80. doi: 10.2174/0929866023409039.

DOI:10.2174/0929866023409039

PMID:12141927

Abstract

Earthworm fibrinolytic enzyme III-1 (EFE-III-1) was prepared to couple with cross-linking agarose activated by 1,'-Carbonyl- diimidazole (CDI) in this study. Although the activity of the immobilized protease decreased to approximately 64% of the native enzyme, the activity of EFE-III-1 coupled with the resin activated by CDI was higher than that activated by cyanogen bromide (CNBr). The immobilized protease was experimentally demonstrated to hydrolyze IgG, albumin and creatine kinase, besides fibrin(ogen) and plasmin(ogen), suggesting that EFE had a broad substrate specificity.

摘要

本研究制备了蚯蚓纤溶酶III-1（EFE-III-1），使其与经1'-羰基二咪唑（CDI）活化的交联琼脂糖偶联。虽然固定化蛋白酶的活性降至天然酶的约64%，但与经CDI活化的树脂偶联的EFE-III-1的活性高于经溴化氰（CNBr）活化的。实验证明，除了纤维蛋白（原）和纤溶酶（原）外，固定化蛋白酶还能水解免疫球蛋白、白蛋白和肌酸激酶，这表明EFE具有广泛的底物特异性。