Isolation and Characterization of a Prolidase from Streptococcus cremoris H61
スポンサーリンク
概要
- 論文の詳細を見る
A prolidase with a molecular weight of 43, 000 was purified to homogeneity from a cell-free extract of Streptococcus cremoris H61. The optimum pH of the enzyme was in the range of 6.5 to 7.5. The hydrolyzing activity was specific for dipeptides of the X-Pro type. Kinetic constants for 4 dipeptides (Leu-Pro, Phe-Pro, Val-Pro and Ala-Pro) were estimated. Km values were not very different for these substrates, but Vmax values were quite different (Leu-Pro> Phe-Pro, Val-Pro> Ala-Pro). The enzyme was activated by cobalt ion and inactivated by metal-chelating agents or with 2-mercaptoethanol.
- 社団法人 日本農芸化学会の論文
著者
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Yamauchi Kunio
Department Of Agricultural Chemistry The University Of Tokyo
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Azuma Norihiro
Department Of Agricultural Chemistry The University Of Tokyo
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Kaminogawa Shuichi
Department Of Agricultural Chemistry Faculty Of Engineering The University Of Tokyo
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Suzuki Yasunori
Department Of Removable Prosthodontics Tsurumi University School Of Dental Medicine
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KAMINOGAWA Shuichi
Department of Agricultural Chemistry, The University of Tokyo
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HWANG In-Kyu
Department of Agricultural Chemistry, The University of Tokyo
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SUZUKI Yasunori
Department of Agricultural Chemistry, The University of Tokyo
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