コイ肉5'-ヌクレオチダーゼの精製

冨岡 和子; 遠藤 金次

doi:10.2331/suisan.50.1077

コイ肉5'-ヌクレオチダーゼの精製

冨岡和子, 遠藤金次

著者情報

ジャーナルフリー

1984 年 50 巻 6 号 p. 1077-1081

DOI https://doi.org/10.2331/suisan.50.1077

詳細

発行日: 1984/06/25 受付日: - J-STAGE公開日: 2008/02/29 受理日: 1983/10/27 早期公開日: - 改訂日: -
訂正情報
訂正日: 2008/02/29 訂正理由: - 訂正箇所: 論文タイトル訂正内容: 訂正前 : コイ肉5′-ヌクレオチダーゼの精製
訂正後 : コイ肉5'-ヌクレオチダーゼの精製

訂正日: 2008/02/29 訂正理由: - 訂正箇所: 論文抄録訂正内容: Wrong : An enzyme which catalyzes the hydrolysis of 5′-IMP to inosine and inorganic phosphate was solubilized from skeletal muscle of carp Cyprinus carpio with a detergent, Emulgen 109P, and was purified by ammonium sulfate fractionation, two steps of affinity chromatography on Concanavalin A-Sepharose and 5′-AMP Sepharose 4B. The purified enzyme was homogeneous on disc gel electrophoresis. An apparent molecular weight of the purified enzyme was estimated to be 24×10⁴ by gel filtration with Sephadex G-200 in the presence of the detergent. The enzyme was found to be a 5′-nucleotidase (EC 3. 1. 3. 5) on the basis of its substrate specificity.
Right : An enzyme which catalyzes the hydrolysis of 5'-IMP to inosine and inorganic phosphate was solubilized from skeletal muscle of carp Cyprinus carpio with a detergent, Emulgen 109P, and was purified by ammonium sulfate fractionation, two steps of affinity chromatography on Concanavalin A-Sepharose and 5'-AMP Sepharose 4B. The purified enzyme was homogeneous on disc gel electrophoresis. An apparent molecular weight of the purified enzyme was estimated to be 24×10⁴ by gel filtration with Sephadex G-200 in the presence of the detergent. The enzyme was found to be a 5'-nucleotidase (EC 3. 1. 3. 5) on the basis of its substrate specificity.

訂正日: 2008/02/29 訂正理由: - 訂正箇所: PDFファイル訂正内容: -

抄録

An enzyme which catalyzes the hydrolysis of 5'-IMP to inosine and inorganic phosphate was solubilized from skeletal muscle of carp Cyprinus carpio with a detergent, Emulgen 109P, and was purified by ammonium sulfate fractionation, two steps of affinity chromatography on Concanavalin A-Sepharose and 5'-AMP Sepharose 4B. The purified enzyme was homogeneous on disc gel electrophoresis. An apparent molecular weight of the purified enzyme was estimated to be 24×10⁴ by gel filtration with Sephadex G-200 in the presence of the detergent. The enzyme was found to be a 5'-nucleotidase (EC 3. 1. 3. 5) on the basis of its substrate specificity.

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