Angiotensin-I Converting Enzyme Inhibitory Peptide Derived from Porcine Skeletal Muscle Myosin and Its Antihypertensive Activity in Spontaneously Hypertensive Rats
| Main Authors: | Katayama, K., Jamhari, Jamhari, Mori, T., Kawahara, S., Miake, K., kodama, Y., Sugiyama, M., Kawamura, Y., Nakayama, T., Maruyama, M., Muguruma, M. |
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| Format: | Article NonPeerReviewed application/pdf |
| Bahasa: | eng |
| Terbitan: |
Institude of Food Technologists
, 2007
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| Subjects: | |
| Online Access: |
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 |
Daftar Isi:
- 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