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Porcine Skeletal Muscle Troponin Is a Good Source of Peptides with Angiotensin-I Converting Enzyme Inhibitory Activity and Antihypertensive Effects in Spontaneously Hypertensive Rats

In the search for novel peptides that inhibit the angiotensin I-converting enzyme (ACE), porcine skeletal troponin was hydrolyzed with pepsin, and the products were subjected to various types of chromatography to isolate active peptides. Glu-Lys-Glu-Arg-Glu-Arg-Gln (EKERERQ) and Lys-Arg-Gln-Lys-Tyr-...

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Bibliographic Details
Published in:Journal of agricultural and food chemistry 2008-01, Vol.56 (2), p.355-360
Main Authors: Katayama, Kazunori, Anggraeni, Henny Endah, Mori, Takahiro, Ahhmed, Abdulatef M, Kawahara, Satoshi, Sugiyama, Masaaki, Nakayama, Tatsuo, Maruyama, Masugi, Muguruma, Michio
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Language:English
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Summary:In the search for novel peptides that inhibit the angiotensin I-converting enzyme (ACE), porcine skeletal troponin was hydrolyzed with pepsin, and the products were subjected to various types of chromatography to isolate active peptides. Glu-Lys-Glu-Arg-Glu-Arg-Gln (EKERERQ) and Lys-Arg-Gln-Lys-Tyr-Asp-Ile (KRQKYDI) were identified as active peptides, and their 50% inhibitory concentrations were found to be 552.5 and 26.2 µM, respectively. These are novel ACE inhibitory peptides, and the activity of KRQKYDI was the strongest among previously reported troponin-originated peptides. KRQKYDI was slowly hydrolyzed by treatment with ACE, and kinetic studies indicated that this peptide was a competitive inhibitor of the enzyme. When KRQKYDI was administered orally to spontaneously hypertensive rats (SHR) at a dose of 10 mg/kg, a temporary antihypertensive activity was observed at 3 and 6 h after administration.
ISSN:0021-8561
1520-5118
DOI:10.1021/jf071408j