König K G, Hasselbach W
Z Naturforsch C Biosci. 1984 Mar-Apr;39(3-4):282-8. doi: 10.1515/znc-1984-3-414.
The effect of pressure on the calcium dependent hydrolysis of para-nitrophenyl phosphate by the calcium transport enzyme of the sarcoplasmic reticulum was studied under different conditions: temperature, solutes, substrate and ion concentrations. The calcium transport enzyme exhibits a large positive activation volume which does neither depend on the enzyme's inhibition by high salt concentrations nor its activation by ethylene glycol. The activation volume further proves to be pressure-independent but exhibits a pronounced negative temperature coefficient. The volume changes connected with the entrance of para-nitrophenyl phosphate, calcium or magnesium ions into the substrate ion complex are quite small, indicating that the transfer of water connected with the binding of these ligands is compensated by volume changes of the protein, accompanying the transition of the enzyme from its activated into its ground state.
在不同条件下（温度、溶质、底物和离子浓度），研究了压力对肌质网钙转运酶催化对硝基苯磷酸酯钙依赖性水解的影响。钙转运酶表现出较大的正活化体积，该体积既不依赖于高盐浓度对酶的抑制作用，也不依赖于乙二醇对酶的激活作用。进一步证明活化体积与压力无关，但表现出明显的负温度系数。与对硝基苯磷酸酯、钙或镁离子进入底物离子复合物相关的体积变化非常小，这表明与这些配体结合相关的水的转移被蛋白质的体积变化所补偿，伴随着酶从活化状态转变为基态。
