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Angiotensin‐I Converting Enzyme Inhibitory Peptide Derived from Porcine Skeletal Muscle Myosin and Its Antihypertensive Activity in Spontaneously Hypertensive Rats
Author(s) -
Katayama K.,
Mori T.,
Kawahara S.,
Miake K.,
Kodama Y.,
Sugiyama M.,
Kawamura Y.,
Nakayama T.,
Maruyama M.,
Muguruma M.
Publication year - 2007
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1750-3841.2007.00571.x
Subject(s) - peptide , chemistry , pepsin , myosin , myosin light chain kinase , enzyme , hydrolysis , renin–angiotensin system , angiotensin converting enzyme , inhibitory postsynaptic potential , biochemistry , angiotensin ii , chromatography , endocrinology , biology , receptor , blood pressure
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.