IN recent work Davies [1934] found that the autolysed extracts of liver and spleen hydrolyse sodium /-glycerophosphate at two different optima of acidity, namely PH 45-5 and PH 8*9, and he expressed the opinion that there were two different phosphatases; however, it was not possible for him to purify the extracts in such a way as to obtain from them two fractions each containing one of the two distinct enzymes.An analogous fact had been observed for the phosphatases of hog kidney by Kurata [1931] who had succeeded in obtaining, by adsorption processes and from the same starting material, two different enzymic solutions, one having an optimum of phosphatase activity at PH 3, the other at PH 9.Recently some Japanese authors of Akamatsu's school [Usawa, 1932; Munemura, 1933, etc.] came to the conclusion that the enzymes which hydrolyse the monoesters of phosphoric acid belong to three types:
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Belfanti et al. (1935) studied this question.
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