Reduction in Water Activity Greatly Retards the Phosphoryl Transfer from ATP to Enzyme Protein in the Catalytic Cycle of Sarcoplasmic Reticulum Ca2+-ATPase

This publication has 33 references indexed in Scilit:

• Characterization of the substrate-induced conformational change of N-iodoacetyl-N′-(5-sulfo-1-naphthyl)ethylenediamine-labeled sarcoplasmic reticulum Ca2+-ATPase by using different kinds of substrate
  Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990
• Role of water in the energy of hydrolysis of phosphate compounds — energy transduction in biological membranes
  Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1989
• Two Ca2+ ATPase genes: Homologies and mechanistic implications of deduced amino acid sequences
  Cell, 1986
• Evaluation of H₂O activity in the free or phosphorylated catalytic site of Ca²⁺‐ATPase
  FEBS Letters, 1983
• Role of water, hydrogen ion, and temperature on the synthesis of adenosine triphosphate by the sarcoplasmic reticulum adenosine triphosphatase in the absence of a calcium ion gradient
  Biochemistry, 1980
• Stimulatory and Inhibitory Effects of Dimethyl Sulfoxide and Ethylene Glycol on ATPase Activity and Calcium Transport of Sarcoplasmic Membranes
  European Journal of Biochemistry, 1977
• A 31‐residue tryptic peptide from the active site of the [Ca⁺⁺]‐transporting adenosine triphosphatase of rabbit sarcoplasmic reticulum
  FEBS Letters, 1976
• ATP Formation from ADP and a Phosphorylated Intermediate of Ca2+-Dependent ATPase in Fragmented Sarcoplasmic Reticulum*
  The Journal of Biochemistry, 1970
• Reaction Mechanism of the Ca++-dependent ATPase of Sarcoplasmic Reticulum from Skeletal Muscle*
  The Journal of Biochemistry, 1967
• ADENOSINE TRIPHOSPHATE-LINKED CONCENTRATION OF CALCIUM IONS IN A PARTICULATE FRACTION OF RABBIT MUSCLE
  The Journal of cell biology, 1962