Digestion of Peptides from Sardine Muscle That Inhibit Angiotensin I Converting Enzyme by Intestinal Enzymes of Pigs
| Autor: | Hideki Matsuda, Yutaka Osajima, Hideo Morita, Toshinori Nagaoka, Katsuhiro Osajima, Toshiyuki Ishizaki |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
chemistry.chemical_classification
animal structures Chromatography Intestinal enzymes integumentary system Sardine Medicine (miscellaneous) Peptide Angiotensin I converting enzyme Intestinal fluid Biochemistry chemistry Chemistry (miscellaneous) embryonic structures Ic50 values Digestion Food Science Biotechnology |
| Zdroj: | Journal of the agricultural chemical society of Japan. 66:1645-1647 |
| ISSN: | 1883-6844 0002-1407 |
| Popis: | Three peptides (I:Leu-Lys-Leu, II:Val-Lys-Ala-Gly-Phe, and III: Lys-Val-Leu-Ala-Gly-Met) from a hydrolyzate of sardine muscle and that inhibited angiotensin I converting enzyme were digested with the intestinal fluid of pigs. The IC50 values of II and III were decreased to 56% and 66% of the original value, respectively, after digestion. Peptide I was not digested. Five peptide fragments were isolated from the peptide digests by high-pressure liquid chromatography. By the Edman procedure, peptide II digest was found to contain the fragments Val-Lys-Ala-Gly and Gly-Phe, and peptide III digest was found to contain the fragments Ala-Gly-Met, Lys-Val-Leu-Ala-Gly, and Lys-Val-Leu. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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