Chemical Modification of Tryptophan and Histidine Residues in Lipoprotein Lipase from Pseudomonas fluorenscens
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概要
- 論文の詳細を見る
Lipoprotein lipase (glycerol ester hydrolase ; EC 3.1.1.3) from Pseudomonas fluorescens was oxidized with N-bromosuccinimide at 37°. One mol of tryptophan residue per mol of enzyme was oxidized, but the enzymatic activity was unaffected. The enzyme was inactivated by photooxidation in the presence of methylene blue, and the inactivation was pH-dependent. In addition, the decrease in the enzymatic activity was accompanied by the loss of a histidine residue. It appears that the histidine residue in involved in the catalytic activity of the enzyme.
- 社団法人日本薬学会の論文
- 1980-09-25
著者
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杉浦 衛
Gifu Pharmaceutical University
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杉浦 衛
Tokyo College Of Pharmacy
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及川 勉
東京薬科大学
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及川 勉
Tokyo College of Pharmacy
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杉浦 衛
Gifu College Of Pharmacy
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