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Induction of angiotensin-converting enzyme inhibitory activity by acid-limited proteolysis of glyceraldehyde 3-phosphate dehydrogenase

1989; Elsevier BV; Volume: 161; Issue: 2 Linguagem: Inglês

10.1016/0006-291x(89)92620-x

1090-2104

Yasuhiro Kohama, Hiroaki Oka, Kohji Yamamoto, Tetsuyuki Teramoto, Masaru Okabe, TSUTOMU MIMURA, Yasukazu Nagase, Yoshiyuki Chiba, Takao Fujita,

Insect Utilization and Effects

Angiotensin-converting enzyme (ACE) inhibitors were excised from glyceraldehyde 3-phosphate dehydrogenase (GAPDH) preparations of tuna and porcine muscles by heating at 120°C for 5 min in 1 M AcOH-20 mM HCl. The inhibitors were then purified by successive chromatographies. The final product from tuna was identified as Pro-Thr-His-Ile-Lys-Trp-Gly-Asp, which was the ACE inhibitor obtained from tuna muscle [Kohama et al. (1988) Biochem. Biophys. Res. Commun. 155, 332–337]. The porcine ACE inhibitor was found to be Pro-Ala-Asn-Ile-Lys-Trp-Gly-Asp, which was identical to the porcine muscle GAPDH peptide 79–86. These results strongly suggested that the ACE inhibitory octapeptides derived from GAPDH proteins by acid-limited proteolysis at Asp-Pro and Asp-Ala peptide bonds.