Biological properties of angiotensin-converting enzyme inhibitor derived from tuna muscle
| Autor: | Shigeru Matsumoto, Mikio Satake, Takefumi Miyamoto, Yasuhiro Kohama, Toshito Nakagawa, Hiroaki Oka, Toshikazu Takane, Yasukazu Nagase, Takao Fujita, Tsutomu Mimura |
|---|---|
| Rok vydání: | 1989 |
| Předmět: |
Carboxypeptidases A
Guinea Pigs Molecular Sequence Data Bradykinin Angiotensin-Converting Enzyme Inhibitors Peptide Carboxypeptidases In Vitro Techniques chemistry.chemical_compound Non-competitive inhibition Chlorides Animals Amino Acid Sequence Pharmacology chemistry.chemical_classification biology Tuna Muscles food and beverages Muscle Smooth Angiotensin-converting enzyme Biological activity Kinetics Zinc chemistry Biochemistry Zinc Compounds Enzyme inhibitor biology.protein Carboxypeptidase A Cattle Rabbits Oligopeptides human activities Muscle Contraction |
| Zdroj: | Journal of Pharmacobio-Dynamics. 12:566-571 |
| ISSN: | 1881-1353 0386-846X |
| DOI: | 10.1248/bpb1978.12.566 |
| Popis: | A novel inhibitor of angiotensin-converting enzyme (ACE) derived from tuna muscle, Pro-Thr-His-Ile-Lys-Trp-Gly-Asp (tuna AI), was chemically synthesized, and its biological properties were investigated. Synthetic tuna AI was found to be chemically and biologically indistinguishable from the native one. Tuna AI inhibited rabbit lung ACE non-competitively with Ki values of 1.7 and 5.7 microM with substrates, hippuryl-L-histidyl-L-leucine and angiotensin I, respectively. This peptide (5.3 microM) also doubled the effect of bradykinin in the contraction of isolated guinea pig ileum. The peptide did not show zinc chelating activity and carboxypeptidase A inhibitory activity. Thus, tuna AI was found to be a unique ACE inhibitory peptide with non-competitive manner, differing from many naturally occurring peptide ACE-inhibitors. |
| Databáze: | OpenAIRE |
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