Angiotensin-I Converting Enzyme Inhibitory Peptide Derived from Porcine Skeletal Muscle Myosin and Its Antihypertensive Activity in Spontaneously Hypertensive Rats
2007
Katayama, K. | Jamhari | Mori, T. | Kawahara, S. | Miake, K. | Kodama, Y. | Sugiyama, M. | Kawamura, Y. | Nakayama, T. | Maruyama, M. | Muguruma, M.
Crude myosin light chain was extracted from Japanese domestic pork loin and digested with pepsin. Antihypertensive peptide was isolated from this digest as a measure of its inhibitory activity for angiotensin-I converting enzyme (ACE). Through isolation with some chromatographies, a single active fraction was isolated, and it was detected as an octapeptide, Val-Lys-Lys-Val-Leu-Gly-Asn-Pro, from 47th to 54th positions of myosin light chain. The 50% inhibitory concentration of this peptide was 28.5 μM. Kinetic evaluation showed that this peptide was a noncompetitive inhibitor, but it was slowly hydrolyzed by ACE. At the dose of 10 mg/kg, this peptide showed antihypertensive activity after a maximum of 3 h of administration and was estimated as a temporally effective hypotensor.
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