魚類,ホタテガイ,ウサギ筋肉のミオシンとアクチンから合成したアクトミオシンの温度安定性

山下 敬子; 新井 健一; 西田 清義

doi:10.2331/suisan.44.485

Thermo-stabilities of Synthetic Actomyosins in Various Combinations of Myosin and Actin form Fish, Scallop, and Rabbit Muscles

Yoshiko YAMASHITA, Ken-ichi ARAI, Kiyoyoshi NISHITA

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JOURNAL FREE ACCESS

1978 Volume 44 Issue 5 Pages 485-489

DOI https://doi.org/10.2331/suisan.44.485

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Published: May 25, 1978 Received: - Available on J-STAGE: February 29, 2008 Accepted: October 24, 1977 Advance online publication: - Revised: -
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Date of correction: February 29, 2008 Reason for correction: - Correction: ABSTRACT Details: Wrong : Myosin and actin were prepared from fish dorsal, rabbit skeletal, and scallop striated adductor muscles. Actomyosins were synthesized in various combinations of myosin and actin preparations by mixing them in an equal weight ratio. The ATP sensitivity and thermostability of the synthetic actomyosins were studied.
1. All combinations of myosin and actin from fish and rabbit sources gave actomyosins having a high ATP sensitivity, while the combinations of scallop myosin and actin of either fish or scallop produced actomyosins having a lower ATP sensitivity. These results suggest a relatively weak binding of myosin and actin.
2. Judging from the first order rate constant (K_D) of inactivation of Ca²⁺-ATPase, it was found that synthetic actomyosins which contained a definite myosin with various actins maintained exactly the same stability against thermal denaturation, although the synthetic actomyosin is approximately 10 times more stable than its myosin moiety.
3. The thermal inactivation of Ca²⁺-ATPase of actomyosins synthesized from fish and scallop sources, assayed at various KCI concentrations, gave nearly the same rate constants.
Right : Myosin and actin were prepared from fish dorsal, rabbit skeletal, and scallop striated adductor muscles. Actomyosins were synthesized in various combinations of myosin and actin preparations by mixing them in an equal weight ratio. The ATP sensitivity and thermostability of the synthetic actomyosins were studied.
1. All combinations of myosin and actin from fish and rabbit sources gave actomyosins having a high ATP sensitivity, while the combinations of scallop myosin and actin of either fish or scallop produced actomyosins having a lower ATP sensitivity. These results suggest a relatively weak binding of myosin and actin.
2. Judging from the first order rate constant (KD) of inactivation of Ca²⁺-ATPase, it was found that synthetic actomyosins which contained a definite myosin with various actins maintained exactly the same stability against thermal denaturation, although the synthetic actomyosin is approximately 10 times more stable than its myosin moiety.
3. The thermal inactivation of Ca²⁺-ATPase of actomyosins synthesized from fish and scallop sources, assayed at various KCI concentrations, gave nearly the same rate constants.

Date of correction: February 29, 2008 Reason for correction: - Correction: PDF FILE Details: -

Abstract

Myosin and actin were prepared from fish dorsal, rabbit skeletal, and scallop striated adductor muscles. Actomyosins were synthesized in various combinations of myosin and actin preparations by mixing them in an equal weight ratio. The ATP sensitivity and thermostability of the synthetic actomyosins were studied.
1. All combinations of myosin and actin from fish and rabbit sources gave actomyosins having a high ATP sensitivity, while the combinations of scallop myosin and actin of either fish or scallop produced actomyosins having a lower ATP sensitivity. These results suggest a relatively weak binding of myosin and actin.
2. Judging from the first order rate constant (KD) of inactivation of Ca²⁺-ATPase, it was found that synthetic actomyosins which contained a definite myosin with various actins maintained exactly the same stability against thermal denaturation, although the synthetic actomyosin is approximately 10 times more stable than its myosin moiety.
3. The thermal inactivation of Ca²⁺-ATPase of actomyosins synthesized from fish and scallop sources, assayed at various KCI concentrations, gave nearly the same rate constants.

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