"INVERSE SUBSTRATES" FOR TRYPSIN-LIKE ENZYMES
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概要
- 論文の詳細を見る
"Inverse substrates" for bovine thrombin and human plasmin were demonstrated. "Inverse substrates" for the enzymes are characterized as specific substrates in which the arrangement of site-specific group is reversed compared to that of normal substrate, e.g., a cationic center is included in their leaving group instead of being in their acyl moiety (K. Tanizawa, Y. Kasaba, Y. Kanaoka, J. Am. Chem. Soc. 99,4485-4488). Kinetic characteristics of thrombin, plasmin and trypsin toward "inverse substrates"were compared. Based on these observations, differences in active centers of the trypsin homologs were discussed. Behavior of p- and m-hydroxyphenylguanidine derivatives as new "inverse substrates" for trypsin was also reported.
- 公益社団法人日本薬学会の論文
著者
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Kanaoka Yuichi
Faculty Of Pharmaceutical Sciences Hokkaido University
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TANIZAWA Kazutaka
Faculty of Pharmaceutical Sciences, Health Sciences University of Hokkaido
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NOZAWA MASAYUKI
Faculty of Pharmaceutical Sciences, Hokkaido University
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KANAOKA Yuichi
Faculty of Pharmaceutical Sciences, Hokkaido University
関連論文
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