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Reversible MM-creatine kinase binding to cardiac myofibrils

Reversible MM-creatine kinase binding to cardiac myofibrils A. SAKS, GUY VASV. ELIZAROVA. Reuersible MM-creatine kinase binding to cardiac myofibrils. Am. J. Physiol. 253 (Cell Physiol. 22): C444-C455,1987.-Skinned rat papillary muscles and purified preparations of rat cardiac myofibrils were used to study the nature of the interaction of creatine kinase with cardiac myofibrils. High activity of creatine kinase (2 IU/mg protein in fibers and 0.9 IU/mg in purified myofibrils) was due mostly to reversibly bound enzyme. This activity could be removed and rebound. The process of creatine kinase rebinding was characterized by apparent K, value of 0.14 mg/ml (-2 x 10s6 M). Rebinding of creatine kinase to cardiac myofibrils restored the phenomenon of functional compartmentation of adenine nucleotides in myofibrillar space and restored the ability of phosphocreatine to decrease the rigor tension in the presence of MgADP. The physiological experiments with quick length changes showed that rebinding of creatine kinase to skinned papillary muscle also restored Ca sensitivity, increased maximal tension development, decreased stiffness, and restored the tension recovery after quick length changes in muscle under condition of inhibition of endogenous creatine kinase by Lfluoro2,4dinitrobenzene. It is concluded that creatine kinase reversibly bound to cardiac myofibrils is involved in the energy supply for cardiac contraction. VENTURA-CLAPIER, http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png AJP - Cell Physiology The American Physiological Society

Reversible MM-creatine kinase binding to cardiac myofibrils

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Publisher
The American Physiological Society
Copyright
Copyright © 1987 the American Physiological Society
ISSN
0363-6143
eISSN
1522-1563
Publisher site
See Article on Publisher Site

Abstract

A. SAKS, GUY VASV. ELIZAROVA. Reuersible MM-creatine kinase binding to cardiac myofibrils. Am. J. Physiol. 253 (Cell Physiol. 22): C444-C455,1987.-Skinned rat papillary muscles and purified preparations of rat cardiac myofibrils were used to study the nature of the interaction of creatine kinase with cardiac myofibrils. High activity of creatine kinase (2 IU/mg protein in fibers and 0.9 IU/mg in purified myofibrils) was due mostly to reversibly bound enzyme. This activity could be removed and rebound. The process of creatine kinase rebinding was characterized by apparent K, value of 0.14 mg/ml (-2 x 10s6 M). Rebinding of creatine kinase to cardiac myofibrils restored the phenomenon of functional compartmentation of adenine nucleotides in myofibrillar space and restored the ability of phosphocreatine to decrease the rigor tension in the presence of MgADP. The physiological experiments with quick length changes showed that rebinding of creatine kinase to skinned papillary muscle also restored Ca sensitivity, increased maximal tension development, decreased stiffness, and restored the tension recovery after quick length changes in muscle under condition of inhibition of endogenous creatine kinase by Lfluoro2,4dinitrobenzene. It is concluded that creatine kinase reversibly bound to cardiac myofibrils is involved in the energy supply for cardiac contraction. VENTURA-CLAPIER,

Journal

AJP - Cell PhysiologyThe American Physiological Society

Published: Sep 1, 1987

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