Porcine skeletal muscle troponin is a good source of peptides with angiotensin-I converting enzyme inhibitory activity and anti hypertensive effects in spontaneously hypertensive rats

Katayama K., Anggraeni H. E., Mori T., Ahhmed A., Kawahara S., SUGIYAMA M., ...Daha Fazla

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, cilt.56, sa.2, ss.355-360, 2008 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 56 Sayı: 2
  • Basım Tarihi: 2008
  • Doi Numarası: 10.1021/jf071408j
  • Dergi Adı: JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.355-360
  • Yıldız Teknik Üniversitesi Adresli: Hayır

Özet

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-lle (KRQKYDI) were identified as active peptides, and their 50% inhibitory concentrations were found to be 552.5 and 26.2 mu M, 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.