Hydrogen ion buffers and enzymatic activity: Myosin B adenosinetriphosphatase

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Hydrogen ion buffers and enzymatic activity: myosin B adenosinetriphosphatase.

The production of hydrogen ions during the hydrolysis of ATP by myosin B and the consequent fall in pH can produce alterations in enzymatic activity directly, or by influencing Ca ion concentrations controlled by metal-chelate systems. Adequate hydrogen ion buffer systems can limit pH changes to acceptable levels. However, several commonly used hydrogen ion buffers have been reported to have sp...

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Cardiac myosin adenosinetriphosphatase activity. Modifying factors and comparison with skeletal muscle myosin adenosinetriphosphatase activity.

Cardiac myosin prepared by any one of a number of modifications of the basic Szent-Gyorgyi method and cardiac myosin prepared by the lithium chloride-ammonium sulfate technique differ in two important respects: 1) SzentGyorgyi-prepared myosin solutions are inhomogeneous by both chemical and immunologic criteria; 2) the ATPase activity of Szent-Gyorgyi-prepared myosin is low in comparison to lit...

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Cardiac Myosin Adenosinetrlphosphatase Activity MODIFYING FACTORS AND COMPARISON WITH SKELETAL MUSCLE MYOSIN ADENOSINETRIPHOSPHATASE ACTIVITY

Cardiac myosin prepared by any one of a number of modifications of the basic Szent-Gyorgyi method and cardiac myosin prepared by the lithium chloride-ammonium sulfate technique differ in two important respects: 1) SzentGyorgyi-prepared myosin solutions are inhomogeneous by both chemical and immunologic criteria; 2) the ATPase activity of Szent-Gyorgyi-prepared myosin is low in comparison to lit...

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Cardiac myosin adenosinetriphosphatase of rat and mouse. Distinctive enzymatic properties compared with rabbit and dog cardiac myosin.

Cardiac myosin obtained from rats and mice (smaller animals) had a higher adenosinetriphosphatase (ATPase) activity in the presence of calcium ions (Ca) than did cardiac myosin from rabbits and dogs (larger animals). Structural differences between the two types of cardiac myosin were suggested by the lower apparent activation energy of the Caactivated ATPase reaction catalyzed by cardiac myosin...

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Effect of pH and Urea on the Optical Rotation, Viscosity, and Adenosinetriphosphatase Activity of Myosin A*

Earlier studies in this laboratory (1) and by other workers (Z-4) have suggested that the effect of alkaline pH and urea on myosin resulted in major structural alterations in the molecule. Many of these studies were concerned with the attempt at the isolation of subunits or small polypeptide fragments by the treatment of myosin with high urea concentrations for long periods of time or by exposu...

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ژورنال

عنوان ژورنال: Archives of Biochemistry and Biophysics

سال: 1968

ISSN: 0003-9861

DOI: 10.1016/0003-9861(68)90027-1