エゾアワビ筋肉のAMP deaminaseについて

関 伸夫

doi:10.2331/suisan.37.871

関伸夫

著者情報

ジャーナルフリー

1971 年 37 巻 9 号 p. 871-876

DOI https://doi.org/10.2331/suisan.37.871

詳細

発行日: 1971/09/25 受付日: - J-STAGE公開日: 2008/02/29 受理日: 1971/03/05 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: 論文抄録訂正内容: Wrong : AMP deaminase, which catalyzes the deamination of AMP to form IMP and NH₃, has been known to be widely distributed in various kinds of animal tissue, however, its presence in the muscles of some invertebrates such as mollusca has been questioned.
The author has detected AMP deaminase activity in the muscle of the abalone, Haliotis discus hannai, and partially purified the enzyme by high speed centrifugation, ethanol fractionation, Li₂SO₄ precipitation and chromatography on DEAE cellulose.
The partially purified enzyme is rapidly inactivated in the absence of ATP by dialysis and heat. ATP is considered to activate and simultaneously to stabilize this enzyme effectively. The optimum pH was found to be near pH 6.4 in citrate Tris buffer. The enzyme is specific for 5′-AMP.
Right : AMP deaminase, which catalyzes the deamination of AMP to form IMP and NH₃, has been known to be widely distributed in various kinds of animal tissue, however, its presence in the muscles of some invertebrates such as mollusca has been questioned.
The author has detected AMP deaminase activity in the muscle of the abalone, Haliotis discus hannai, and partially purified the enzyme by high speed centrifugation, ethanol fractionation, Li₂SO₄ precipitation and chromatography on DEAE cellulose.
The partially purified enzyme is rapidly inactivated in the absence of ATP by dialysis and heat. ATP is considered to activate and simultaneously to stabilize this enzyme effectively. The optimum pH was found to be near pH 6.4 in citrate Tris buffer. The enzyme is specific for 5'-AMP.

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

AMP deaminase, which catalyzes the deamination of AMP to form IMP and NH₃, has been known to be widely distributed in various kinds of animal tissue, however, its presence in the muscles of some invertebrates such as mollusca has been questioned.
The author has detected AMP deaminase activity in the muscle of the abalone, Haliotis discus hannai, and partially purified the enzyme by high speed centrifugation, ethanol fractionation, Li₂SO₄ precipitation and chromatography on DEAE cellulose.
The partially purified enzyme is rapidly inactivated in the absence of ATP by dialysis and heat. ATP is considered to activate and simultaneously to stabilize this enzyme effectively. The optimum pH was found to be near pH 6.4 in citrate Tris buffer. The enzyme is specific for 5'-AMP.

責任著者(Corresponding author)

訂正情報

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