Angiotensin-I converting enzyme inhibitory peptide derived from porcine skeletal muscle myosin and its antihypertensive activity in spontaneously hypertensive rats |
| |
| Authors: | Katayama K Jamhari,Mori T,Kawahara S,Miake K,Kodama Y,Sugiyama M,Kawamura Y,Nakayama T,Maruyama M,Muguruma M |
| |
| Affiliation: | Authors Katayama, Jamhari, Mori, Kawahara, and Muguruma are with Dept. of Biochemistry and Applied Biosciences, Faculty of Agriculture, Univ. of Miyazaki, Miyazaki 889-2192, Japan. Authors Miake, Kodama, and Sugiyama are with Marudai Food Co. Ltd., Takatsuki, Osaka 569-8577, Japan. Author Kawamura is with Graduate School of Agriculture, Kinki Univ., Nara 3327-204 Japan. Authors Nakayama and Maruyama are with Faculty of Medicine, Univ. of Miyazaki, Kiyotake, Miyazaki 889-1692, Japan. Direct inquiries to author Muguruma (E-mail: ). |
| |
| Abstract: | ABSTRACT: 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. |
| |
| Keywords: | angiotensin I-converting enzyme inhibitory peptide antihypertensive activity porcine skeletal myosin light chain protease digestion spontaneously hypertensive rat |
| 本文献已被 PubMed 等数据库收录！ |
|
