Abstract
The properties of the plasma acid phosphatases of patients suffering from primary hyperparathyroidism, osteopetrosis, Gaucher's disease and metastatic carcinoma of the prostate have been evaluated and compared. In all cases with increased total acid phosphatase activity, two or three maxima of activity were found in the acid pH range using 0.2 M acetate buffer. Starch gel electrophoresis showed separation of 3 fractions in primary hyperparathyroidism, osteopetrosis and normal controls, 4 in carcinoma of the prostate, and 5 in Gaucher's disease. The substrates phenylphosphate, β-glycerophosphate and α-glycerophosphate are hydrolysed in the order listed, with decreasing velocity in normal controls, osteopetrosis, Gaucher's disease and prostate carcinoma. α-Glycerophosphate is hydrolysed preferentially in primary hyperparathyroidism. These phosphatases are further differentiated with the aid of various effectors. 5.10 −3 M l-tartrate inactivates the enzymes to 90% in cases of metastatic prostate carcinoma, to 40% in osteopetrosis. 10 −4 M solution of cystein decreases the activity of plasma acid phosphatases to about 70% at pH 5.1–5.3 in osteopetrosis, but activates the enzymes to 70% in Gaucher's disease and to 30% in carcinoma of the prostate. EDTA, 2.5 · 10 −3 M solution increased the acid phosphatase activity to 40% in primary hyperparathyroidism, but had no effect on the enzyme activity in all the other investigated cases.
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