@article{oai:ngu.repo.nii.ac.jp:00000398,
 author = {酒井, 淳一 and 中野, 貴博 and 齋藤, 健治 and 山本, 親 and 村瀬, 豊 and 岡田, 忠 and 箭頭, 真理子 and 竹田, 忠紘},
 issue = {2},
 journal = {名古屋学院大学論集　人文・自然科学篇, THE NAGOYA GAKUIN DAIGAKU RONSHU; Journal of Nagoya Gakuin University; HUMANITIES and NATURAL SCIENCES},
 month = {Jan},
 note = {Recently, we determined the primary structure of a thrombin-like protease isolated from the venom of Agkistrodon halys brevicaudus stejneger snake. The protease was found to be a single chain glycoprotein with a molecular weight of 32 kDa, containing 18% carbohydrates. The carbohydrate chain binding positions, Asn81, 99 and 148, were located in the neighbourhood of an active site cleft. In this study, the enzymatic property of the deglycosylated protease was compared to the intact protease in order to elucidate the role of the carbohydrate chain. The deglycosylation of the protease was carried out by glycosidase treatment and the deglycosylated protease with a molecular weight of 26.5 kDa was obtained. The intact protease converted human fibrinogen to fibrin. Fibrinopeptide A, B and Bβ1-42 were released during fibrin clot formation. The deglycosylated protease also formed the fibrin clot. Fibrinopeptide A primarily released although the release of the fibrinopeptide B and Bβ1-42 was significantly reduced. Removal of the carbohydrate moiety resulted in a decrease in these fragment releases, suggesting that the access of the fibrinogen Bβ chain to the active site was restricted by the deglycosylation. Thus, the carbohydrate chain may play an important role in the conformational integrity of the active site and also in the interaction between the protease and substrates, especially a large molecular substrate such as fibrinogen.},
 pages = {47--50},
 title = {蛇毒由来トロンビン様セリン酵素に結合する糖鎖の役割},
 volume = {47},
 year = {2011}
}