Additional Evidence for the Identity of Scytalidium lignicolum Acid Proteinases with the Carboxyl Proteinase Group : The Interaction between Angiotensin I and S-PI-Insensitive Acid Proteinases by Means of A Zinc(II)-Dye Complex as a Probe(Biological Chemi
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概要
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S. lignicolum acid proteinases A-1, A-2, and B(S-PI-insensitive) were examined for the structure of the active sites by the method of Nakatani using PAD as a probe. We attempted to screen for substances that release zinc(II)-PAD from the complex of zinc(II)-PAD-S-PI-insensitive acid proteinases. Angiotensin I released zinc(II)-PAD from the complex as well as from the complex of S-PI-sensitive acid proteinases. Angiotensin I is a good substrate for these enzymes regardless of S-PI-sensitivity. These results suggest that the two carboxyl groups capable of binding to zinc(II)-PAD are at the active site regions of S. lignicolum enzymes and that they are involved in their catalytic actions.
- 社団法人日本農芸化学会の論文
- 1986-08-23
著者
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ODA Kohei
Department of Applied Biology, Kyoto Institute of Technology
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Murao Sawao
Department of Agricultural Chemistry, College of Agriculture, University of Osaka Prefecture
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Oda Kohei
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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Murao Sawao
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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