Chemical Modification of Urokinase with Bis-imidoesters and Properties of the Intramolecularly Cross-linked Enzyme(Biological Chemistry)
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概要
- 論文の詳細を見る
To prepare a chemically modified urokinase that does not dissociate into two peptide fragments upon reduction of its disulfide bridge, we cross-linked the enzyme intramolecularly with various bifunctional imidoesters. The enzyme underwent the intramolecular cross-linking most moderately by the reaction at 4℃ for 5hr with 3mM dimethyl suberimidate in 0.1M potassium phosphate buffer (pH 9.0). The cross-linked urokinase isolated by gel filtration with a yield of 25% showed a specific activity of 76,000 International Units/mg protein, which corresponds to 53% of that of the native enzyme. Although the modified enzyme was similar to the native urokinase in some properties such as the autocatalytic self-digestion and the low affinity to fibrin, it showed higher in vivo and in vitro stabilities than the native one.
- 社団法人日本農芸化学会の論文
- 1989-07-23
著者
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TANIZAWA Katsuyuki
The Institute of Scientific and Industrial Research, Osaka University
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SODA Kenji
Laboratory of Microbiology, Institute for Chemical Research, Kyoto University
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Soda Kenji
Laboratory Of Microbial Biochemistry Institute For Chemical Research Kyoto University
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TANIZAWA Katsuyuki
Laboratory of Microbial Biochemistry, Institute for Chemical Research, Kyoto University
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Soda K
Laboratory Of Microbial Biochemistry Institute For Chemical Research Kyoto University
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Tanizawa K
The Institute Of Scientific And Industrial Research Osaka University
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Tanizawa Katsuyuki
Laboratory Of Microbial Biochemistry Institute For Chemical Research Kyoto University
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YOKOIGAWA Kumio
Laboratory of Microbial Biochemistry, Institute for Chemical Research, Kyoto University
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Yokoigawa K
Nara Women's Univ. Nara Jpn
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