Dependence of the pH-optimum of the phosphomonoesterase I on the substrate concentration and on inhibitors and activators

摘要: Abstract 1. The fact is pointed out that according to the p H activity-curve of phosphomonoesterase I from animal organs ferment so highly active at an unphysiological and little in physiological region. 2. For alkaline phosphate it was shown substrate concentration influences position -activity curve. At a low curve shifts neutral It expounded cell concentrations will be low. determination curves chosen generally such as not affect rate reaction. These are comparatively high concentrations, inferences about optimum for phosphatase activity cannot drawn them. 3. By dialysis kidney extracts possible remove inhibitory substance. Before after found same . 4. Phosphomonoesterase could adsorbed kaolin afterwards eluted again. Subsequently enzyme precipitated with ethanol. preparations purified this way contain no other phosphomonoesterases; however, they do pyrophosphatase I. adsorption diphenylmethanol subsequent elution freed pyrophosphatase. purification did 5. influence number cations anions on situation tested. They were have practically influence.