Production of Angiotensin-Converting Enzyme Inhibitors from Baker's Yeast Glyceraldehyde-3-phosphate Dehydrogenase
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概要
- 論文の詳細を見る
Angiotensin-converting enzyme (ACE) inhibitors were excised from the molecule of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) preparation of baker's yeast by heating at 120℃ in 1 M AcOH-20 mM HCl. Three inhibitors were then purified by gel-permeation and reversephase chromatographies. One of the yeast ACE inhibitors, YG-3,was GAPDH peptide 79-89 (Pro-Ala-Asn-Leu-Pro-Trp-Gly-Ser-Ser-Asn-Val, IC_<50> : 18 μM), and contained the sequence homologous to vertebratc ACE inhibitors (GAPDH peptides 79-86 or 81-88). Other inhibitors, YG-1 (Gly-His-Lys-Ile-Ala-Thr-Phe-Gln-Glu-Arg, IC_<50> : 0.4 μM) and YG-2 (Gly-Lys-Lys-Ile-Ala-Thr-Tyr-Gln-Glu-Arg, IC_<50> : 2 μM), corresponded to amino acid residues 68-77 in two different forms of yeast GAPDH, respectively. Their sequences were quite different from those of the venom peptide family. YG-1 was the most potent ACE inhibitor among yeast and vertebrate GAPDH peptides excised by acid-limited proteolysis. Thus, yeast GAPDH seems to be an excellent source of naturally occurring ACE inhibitors.
- 公益社団法人日本薬学会の論文
著者
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OKA Hiroaki
Faculty of Pharmaceutical Sciences, Osaka University
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Yokoyama Kazumasa
Central Research Laboratories Green Cross Corporation Ltd.
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KOHAMA YASUHIRO
Faculty of Pharmaceutical Sciences, Osaka University
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MIMURA TSUTOMU
Faculty of Pharmaceutical Sciences, Osaka University
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Inamori Yoshihiko
Department Of Microbiology Osaka University Of Pharmaceutical Sciences
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Oka H
Faculty Of Pharmaceutical Sciences Osaka University
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Oka Hiroaki
Faculty Of Pharmaceutical Sciences Osaka University
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Mimura T
Faculty Of Pharmaceutical Sciences Osaka University
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Mimura Tsutomu
Faculty Of Pharmaceutical Sciences Osaka University
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Mimura Tsutomu
Division Of Bio-medical And Immunological Chemistry Faculty Of Pharmaceutical Sciences Osaka Univers
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MURAYAMA Norihito
Faculty of Pharmaceutical Sciences, Osaka University
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TERAMOTO Tetsuyuki
Faculty of Pharmaceutical Sciences, Osaka University
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NAGASE Yasukazu
Life Sciences Affairs, Machida Pharmaceutical Co., Ltd.
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NAGASE Yasukazu
Faculty of Pharmaceutical Sciences, Osaka University
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NAKAGAWA Toshito
Faculty of Pharmaceutical Sciences, Osaka University
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TSUJIBO Hiroshi
Faculty of Pharmaceutical Sciences, Osaka University
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INAMORI Yoshihiko
Faculty of Pharmaceutical Sciences, Osaka University
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Oka H
Osaka Univ. Osaka
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Kohama Yasuhiro
Division Of Cellular Physiology Faculty Of Pharmaceutical Sciences Osaka University
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Kohama Yasuhiro
Faculty Of Pharmaceutical Sciences Osaka University
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Kohama Yasuhiro
Division Of Bio-medical And Immunological Chemistry Faculty Of Pharmaceutical Sciences Osaka Univers
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Kayamori Yuzo
Faculty Of Pharmaceutical Sciences Osaka University
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YOKOYAMA Kazumasa
Faculty of Education, Shiga University
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Nakagawa Teruaki
Faculty Of Pharmaceutical Sciences Osaka University:life Science Affairs Mochida Pharmaceutical Co.
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Mimura T
Division Of Bio-medical And Immunological Chemistry Faculty Of Pharmaceutical Sciences Osaka Univers
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Yokoyama K
Faculty Of Education Shiga University
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Nagase Y
Life Sciences Affairs Machida Pharmaceutical Co. Ltd.
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Miyamoto T
Faculty Of Pharmaceutical Sciences Osaka University
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Mimura T
Division Of Bio-medical And Immunological Chemistry Faculty Of Pharmaceutical Sciences Osaka Univers
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Murayama Norihito
Faculty Of Pharmaceutical Sciences Osaka University
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Teramoto Tetsuyuki
Faculty Of Pharmaceutical Sciences Osaka University
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Mimura T
Division Of Bio-medical And Immunological Chemistry Faculty Of Pharmaceutical Sciences Osaka Univers
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Tsujibo Hiroshi
Faculty Of Pharmaceutical Sciences Osaka University
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