Induction of angiotensin-converting enzyme inhibitory activity by acid-limited proteolysis of glyceraldehyde 3-phosphate dehydrogenase.
Angiotensin-converting enzyme (ACE) inhibitors were excised from glyceraldehyde 3-phosphate dehydrogenase (GAPDH) preparations of tuna and porcine muscles by heating at 120 degrees 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.
Kohama
Y
Y
Faculty of Pharmaceutical Sciences, Osaka University, Japan.
Oka
H
H
Yamamoto
K
K
Teramoto
T
T
Okabe
M
M
Mimura
T
T
Nagase
Y
Y
Chiba
Y
Y
Fujita
T
T
D000595:Amino Acid Sequence; D000806:Angiotensin-Converting Enzyme Inhibitors / Q000096:biosynthesis* / Q000302:isolation & purification; D000818:Animals; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism*; D007700:Kinetics; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification / Q000494:pharmacology*; D010447:Peptide Hydrolases / Q000494:pharmacology; D013552:Swine; D014413:Tuna
D000806:Angiotensin-Converting Enzyme Inhibitors; D010446:Peptide Fragments; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D010447:Peptide Hydrolases