Studies on acid hydrolases in adult and foetal tissues. Acid p-nitrophenyl phosphate phosphohydrolases of adult guinea-pig liver

Some tissues contain more than one enzyme exhibiting 'acid-phosphatase' action and the partial separation of such enzymes has been re- ported, e.g. from rat liver (Goodlad & Mills, 1957; Barka, 1961 a, b) and from Escherichia coli (Rogers & Reithel, 1960). Among the factors that make the interpretation of experimental observations on 'acid-phosphatase activity' difficult are (a) in the earlier work, lack of knowledge of the lysosomal sequestering of acid P-glycerophosphate phospho- hydrolase (/3-glycerophosphatase) and the condi- tions in which it is released, (b) the variety of sub- strates used for assay coupled with a lack of in- formation concerning the identity of the enzyme(s) responsible for the hydrolysis of any given substrate and (c) the wide diversity of properties of 'acid phosphatases', both from different tissues within a species and from similar tissues in different species.