Photoaffinity labeling of pepsin.
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概要
- 論文の詳細を見る
Photoaffinity reagents for pepsin [Ala–Gly–Phe(N<SUB>3</SUB>), Gly–Gly–Phe(N<SUB>3</SUB>)–Phe–Gly–OEt, Gly–Gly–Phe–Phe(N<SUB>3</SUB>)–Gly–OEt] were synthesized by a solution method. The pentapeptides were cleaved rapidly at the peptide bond between two aromatic amino acid residues by pepsin. This shows that Phe(N<SUB>3</SUB>) residues of the photoaffinity reagents bind with the S<SUB>1</SUB> or S<SUB>1</SUB>′ site of pepsin. Pepsin was irradiated with photoaffinity reagents and the remaining activity was measured. The pepsin activity was decreased more rapidly in the presence of photoaffinity reagents, compared with that in the absence of photoaffinity reagents. Photoaffinity labeling occured at pH 2.0; however, did not occur at pH 4.0. Photoaffinity labeling of pepsin with <SUP>3</SUP>H-labeled Gly–Gly–Phe(N<SUB>3</SUB>)–Phe–Gly–OEt showed that about 9% of the pepsin bound covalently with the photoaffinity reagent.
- 公益社団法人 日本化学会の論文
著者
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YONEZAWA Hiroo
Department of Chemistry, Faculty of Science, Kagoshima University
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Wada Tetsuya
Department of Chemistry, Faculty of Science, Kagoshima University
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