论文信息 - Rate constants and equilibrium constants for the elementary steps of ATP hydrolysis by beef heart mitochondrial ATPase. - 字舞流文

Rate constants and equilibrium constants for the elementary steps of ATP hydrolysis by beef heart mitochondrial ATPase.

[1] C. Grubmeyer,et al. Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase. Rate constants for elementary steps in catalysis at a single site. , 1982, The Journal of biological chemistry.

[2] C. Grubmeyer,et al. Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase. Rate enhancements resulting from cooperative interactions between multiple catalytic sites. , 1982, The Journal of biological chemistry.

[3] C. Grubmeyer,et al. Cooperatively between catalytic sites in the mechanism of action of beef heart mitochondrial adenosine triphosphatase. , 1981, The Journal of biological chemistry.

[4] C. Grubmeyer,et al. The presence of two hydrolytic sites on beef heart mitochondrial adenosine triphosphatase. , 1981, The Journal of biological chemistry.

[5] J. W. Long,et al. The construction and testing of a simple, slow delivery-rapid quench apparatus. , 1976, Biochemistry.

[6] Y. Sugino,et al. THE SPECIFIC PRECIPITATION OF ORTHOPHOSPHATE AND SOME BIOCHEMICAL APPLICATIONS. , 1964, The Journal of biological chemistry.

[7] J. Sakamoto. Identification of the nucleotide-binding site for ATP synthesis and hydrolysis in mitochondrial soluble F1-ATPase. , 1984, Journal of biochemistry.

[8] J. Chappell,et al. A simple method for the preparation of 32P-labelled adenosine triphosphate of high specific activity , 1964 .