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发表时间：2008-01-01

发表刊物：高等学校化学学报

所属单位：生物工程学院

卷号：29

期号：3

页面范围：542-545

ISSN号：0251-0790

摘要：The peptides can be obtained by enzymatic proteolysis of food proteins and may act as potential physiological regulators of metabolism (luring the intestinal digestion of diet, To investigate bioactive peptides within food proteins, six peptides derived from alpha-chain of hemoglobin were synthesized via peptide solid-phase method. The peptides were purified on Sephadex LH-20 gel chromatography column and detected by RP-HPLC and MS respectively. In, vitro bioactivity of Leu-Gly-Phe-Pro-Thr-Thr-Lys-Thr-Tyr-Phe-Pro-His-Phe showed similar activity(IC50 = 4.76 mu mol/L) in inhibition of angiotensin I-converting enzyme(ACE) compared with that obtained from globin hydro-lysis(IC50 =4. 92 mu mol/L). These results confirm that the peptide inhibitors of ACE, which contain a hydrophobic amino acid at C-terminal with branehed side chain( e. g. Leu, Phe, Pro), are more active. No alpha-glucosidase inhibitory activity was detected. The results indicate that these peptides have a potential antihypertensive effect and possible application in remedy of hypertension.

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