コイ筋原線維Ca-ATPaseの酸変性とKCl濃度の関係

舩津 保浩; 橋本 昭彦; 今野 久仁彦; 新井 健一

doi:10.2331/suisan.56.133

舩津保浩, 橋本昭彦, 今野久仁彦, 新井健一

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ジャーナルフリー

1990 年 56 巻 1 号 p. 133-137

DOI https://doi.org/10.2331/suisan.56.133

詳細

発行日: 1990/01/25 受付日: 1989/08/28 J-STAGE公開日: 2008/02/29 受理日: - 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 : Denaturations of carp myofibrils and myosin induced by changing pH and KCl concentration were studied. Myofibrils and myosin suspension was mixed with maleate-NaOH buffer to set the pH between 4.81 and 6.14 in the presence of various concentrations of KCl (0.1-1.0_M) and stored at 2°C. The first order rate constant (K_D) for inactivation of Ca-ATPase caused by the above treatment was then estimated.
It was thus found that the K_D of myofibrillar Ca-ATPase increased with lowering the pH as well as with increasing KCl concentration. On the other hand, the K_D of myosin Ca-ATPase remained practically unchanged with changing the KCl concentration but increased with lowering the pH, in the same manner as in the case of myofibrils, In addition, the K_D of myosin Ca-ATPase agrecd closely with that of myofibrillar Ca-ATPase in the presence of 1.0_M KCl. These results strongly suggested that the actin part of carp myofibrils was denatured by acid treatment in the presence of 1.0_M KCl, and lost its protective activity against thermal inactivation of myosin Ca-ATPase.
Right : Denaturations of carp myofibrils and myosin induced by changing pH and KCl concentration were studied. Myofibrils and myosin suspension was mixed with maleate-NaOH buffer to set the pH between 4.81 and 6.14 in the presence of various concentrations of KCl (0.1-1.0_M) and stored at 2°C. The first order rate constant (K_D) for inactivation of Ca-ATPase caused by the above treatment was then estimated.
It was thus found that the K_D of myofibrillar Ca-ATPase increased with lowering the pH as well as with increasing KCl concentration. On the other hand, the K_D of myosin Ca-ATPase remained practically unchanged with changing the KCl concentration but increased with lowering the pH, in the same manner as in the case of myofibrils, In addition, the K_D of myosin Ca-ATPase agrecd closely with that of myofibrillar Ca-ATPase in the presence of 1.0M KCl. These results strongly suggested that the actin part of carp myofibrils was denatured by acid treatment in the presence of 1.0M KCl, and lost its protective activity against thermal inactivation of myosin Ca-ATPase.

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

Denaturations of carp myofibrils and myosin induced by changing pH and KCl concentration were studied. Myofibrils and myosin suspension was mixed with maleate-NaOH buffer to set the pH between 4.81 and 6.14 in the presence of various concentrations of KCl (0.1-1.0_M) and stored at 2°C. The first order rate constant (K_D) for inactivation of Ca-ATPase caused by the above treatment was then estimated.
It was thus found that the K_D of myofibrillar Ca-ATPase increased with lowering the pH as well as with increasing KCl concentration. On the other hand, the K_D of myosin Ca-ATPase remained practically unchanged with changing the KCl concentration but increased with lowering the pH, in the same manner as in the case of myofibrils, In addition, the K_D of myosin Ca-ATPase agrecd closely with that of myofibrillar Ca-ATPase in the presence of 1.0M KCl. These results strongly suggested that the actin part of carp myofibrils was denatured by acid treatment in the presence of 1.0M KCl, and lost its protective activity against thermal inactivation of myosin Ca-ATPase.

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