Puritication and Properties of α-Glucosidase from Trichoderma viride
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概要
- 論文の詳細を見る
α-Glucosidase (EC 3.2.1.20) from Trichoderma viride was purified by a procedure including Sephacryl S-200 HR column chromatography, preparative isoelectric focusing, and Superdex 200 HR column chromatography. The enzyme was found to have an apparent molecular weight of 67,000 on SDS/PAGE and 65,000 on gelfiltration, showing that the enzyme is a single peptide. The isoelectric point of the enzyme was 5.0. The enzyme hydrolyzed α-1, 4-glucosidic linkage more rapidly than α-1, 6-glucosidic and α-1, 3-glucosidic link-ages. The enzyme was weakly inhibited by castanospermine.
- 社団法人日本農芸化学会の論文
- 1995-11-23
著者
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Konno Hiroyuki
Department Of Applied Biological Chemistry Faculty Of Agriculture
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Konno Haruyoshi
Research Institute For Bioresources Okayama University
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Yamasaki Yoshiki
Research Institute for Bioresources, Okayama University
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Elbein D.
Department of Biochemistry & Molecular Biology, University of Arkansas for Medical Sciences
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Yamasaki Y
Okayama Univ. Kurashiki Jpn
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Yamasaki Yoshiki
Research Institute For Bioresources Okayama University
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Elbein D.
Department Of Biochemistry & Molecular Biology University Of Arkansas For Medical Sciences
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