Proteolysis of myosin and troponin in human myocardium of elderly subjects.
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概要
- 論文の詳細を見る
Actomyosin was prepared from human myocardium and its protein composition was examined by SDS-polyacrylamide gel electrophoresis. For some preparations, particularly actomyosin isolated from elderly subjects, a high molecular weight (HMW) band (identified as a breakdown product of myosin heavy chain) appeared, while the troponin-T subunit decreased. Myofibril associated protease (MFP) activity showed no significant difference as a function of proteolysis. In agreement with the proteolysis of troponin-T and myosin, the Ca2+ sensitivity of Mg2+-ATPase activity decreased while the extent of the stimulation of Ca2+-ATPase by N-ethylmaleimide remained unchanged. This type of proteolysis would affect the Ca2+-dependent regulation of muscle contraction but not the contractility per se.
- International Heart Journal刊行会の論文
著者
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Matoba Ryoji
Department Of Forensic Medicine Osaka University School Of Medicine
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Wakasugi Choei
Department Of Legal Medicine Osaka University Medical School
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Yoshida Ken-ichi
Department Of Agrobioscience Graduate School Of Agricultural Science Kobe University
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MATOBA Ryoji
Department of Legal Medicine, Saga Medical College
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HANAFUSA Tohru
Department of Legal Medicine, Osaka University Medical School
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