Pressure effects on the interactions of the sarcoplasmic reticulum calcium transport enzyme with calcium and para-nitrophenyl phosphate.
The effect of hydrostatic pressure on calcium dependent p-nitrophenyl phosphate hydrolysis of the sarcoplasmic reticulum calcium transport enzyme has been investigated at different degree of enzyme saturation by calcium and Mg-p-nitrophenyl phosphate to distinguish between activation and binding volumes. The enzyme saturated by both ligands displays a significant dependence of the activation volume on pressure, rising from 20 ml/mol at atmospheric pressure (0.1 MPa) to 80 ml/mol at 100 MPa. At subsaturating concentration of Mg-p-nitrophenyl phosphate an activation volume of 35 ml/mol prevails between 0.1 and 40 MPa. At subsaturating concentration of calcium the activation volume approximates 80 ml/mol in the same pressure range. The binding volume for both substrates is likewise pressure dependent falling from 20 ml/mol to 0 ml/mol for Mg-p-nitrophenyl phosphate and rising from 67 ml/mol to 155 ml/mol for calcium. The pressure dependence of activation and binding volumes is analysed on account of a simplified reaction scheme yielding activation volumes and rate constants for individual reaction steps.
D000818:Animals; D002118:Calcium / Q000378:metabolism*; D000252:Calcium-Transporting ATPases / Q000378:metabolism*; D007700:Kinetics; D008024:Ligands; D008274:Magnesium / Q000378:metabolism; D009132:Muscles / Q000201:enzymology; D009596:Nitrophenols / Q000378:metabolism*; D009943:Organophosphorus Compounds / Q000378:metabolism*; D011312:Pressure; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000201:enzymology*
D008024:Ligands; D009596:Nitrophenols; D009943:Organophosphorus Compounds; C008644:nitrophenylphosphate; D000252:Calcium-Transporting ATPases; D008274:Magnesium; D002118:Calcium