Angiotensin-I Converting Enzyme Inhibitory Peptide Derived from Porcine Skeletal Muscle Myosin and Its Antihypertensive Activity in Spontaneously Hypertensive Rats

• المؤلفون الرئيسيون: Katayama, K., Jamhari, Jamhari, Mori, T., Kawahara, S., Miake, K., kodama, Y., Sugiyama, M., Kawamura, Y., Nakayama, T., Maruyama, M., Muguruma, M.
• التنسيق: مقال NonPeerReviewed
• اللغة: English
• منشور في: Institude of Food Technologists 2007
• الموضوعات: Food technology
• الوصول للمادة أونلاين: https://repository.ugm.ac.id/139182/1/Jurnal%20of%20Food%20Science_Jamhari%20-%201.pdf; https://repository.ugm.ac.id/139182/; http://onlinelibrary.wiley.com/doi/10.1111/jfds.2007.72.issue-9/issuetoc
• المؤسسة: Universitas Gadjah Mada

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 con-verting 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 /iM. 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 antihy¬pertensive activity after a maximum of 3 h of administration and was estimated as a temporally effective hypotensor. Keywords: angiotensin I-converting enzyme inhibitory peptide, antihyperlensive activity, porcine skeletal myosin light chain, protease digestion, spontaneously hypertensive rat