Purification and Characterization of a Basic Amino Acid-Specific Peptidase from Seeds of Jack Bean (Canavalia ensiformis)
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概要
- 論文の詳細を見る
A peptidase was purified from seeds of Canavalia ensiformis by extraction with water, ammonium sulfate precipitation, and successive chromatographies on DEAE-Toyopearl 650M, butyl-Toyopearl 650M, and G-3000 SW columns. The enzyme has an apparent molecular weight of 41,000. Activity is maximal at pH 9 and 60℃. The enzyme hydrolyzed synthetic substrates at Arg-X and Lys-X bonds more rapidly than bovine trypsin did, and did not cleave protein or ester substrates. The enzyme was inhibited by alkylamines and several serine protease inhibitors such as diisopropyl-fluorophosphate, chymostatin, leupeptin, and benzamidine. Cysteine protease-, metalloprotease-, and proteinous trypsin inhibitors were ineffective. Inhibition by alkylamines was dependent on length of the alkyl chains. From the substrate specificity and susceptibility to chemicals, the enzyme is a unique peptidase with trypsin-like specificity.
- 社団法人日本農芸化学会の論文
- 2000-10-23
著者
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Terada Shigeyuki
Department Of Chemistry Faculty Of Science Fukuoka University
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Oshikawa K
Fukuoka Univ. Fukuoka
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Oshikawa Kiyotaka
Department Of Chemistry Faculty Of Science Fukuoka University
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Aoki Kenichi
Department Of Anthropology Faculty Of Science The University Of Tokyo
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Aoki Kenichi
Department Of Chemistry Faculty Of Science Fukuoka University
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YOSHINO Yuuki
Department of Chemistry, Faculty of Science, Fukuoka University
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Yoshino Y
Nagoya Univ. Nagoya Jpn
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Aoki Ken-ichi
Department of Chemistry, Faculty of Science, Fukuoka University
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