Production of angiotensin-converting enzyme inhibitors from baker's yeast glyceraldehyde-3-phosphate dehydrogenase
Autor: | Norihito Murayama, Hiroshi Tsujibo, Hiroaki Oka, Yoshihiko Inamori, Tsutomu Mimura, Toshito Nakagawa, Tetsuyuki Teramoto, Yasuhiro Kohama, Yasukazu Nagase |
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Rok vydání: | 1990 |
Předmět: |
Pharmacology
chemistry.chemical_classification biology medicine.diagnostic_test Proteolysis Molecular Sequence Data Glyceraldehyde-3-Phosphate Dehydrogenases Angiotensin-Converting Enzyme Inhibitors Angiotensin-converting enzyme Peptide Saccharomyces cerevisiae Molecular biology Peptide Fragments Yeast Enzyme stomatognathic system chemistry Biochemistry Enzyme inhibitor biology.protein medicine Amino Acid Sequence Peptide sequence Chromatography High Pressure Liquid Glyceraldehyde 3-phosphate dehydrogenase |
Zdroj: | Journal of Pharmacobio-Dynamics. 13:766-771 |
ISSN: | 1881-1353 0386-846X |
DOI: | 10.1248/bpb1978.13.766 |
Popis: | 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 degrees C in 1 M AcOH-20 mM HCl. Three inhibitors were then purified by gel-permeation and reverse-phase 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, IC50:18 microM), and contained the sequence homologous to vertebrate ACE inhibitors (GAPDH peptides 79-86 or 81-88). Other inhibitors, YG-1 (Gly-His-Lys-Ile-Ala-Thr-Phe-Gln-Glu-Arg, IC50: 0.4 microM) and YG-2 (Gly-Lys-Lys-Ile-Ala-Thr-Tyr-Gln-Glu-Arg, IC50: 2 microM), 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. |
Databáze: | OpenAIRE |
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