Subcellular distribution of low- and high-molecular-weight acid phosphatases.
Acid phosphatases (orthophosphoric-monoester phosphohydrolases (acid optimum), EC 3.1.3.2) of low and high molecular weight were separated by Sephadex G-75 filtration from extracts of rat brain, liver and kidney. The proportion of each phosphatase in the extract depends critically on the method employed for homogenate preparation, and no interconversion between high and low molecular weight forms was detected. In extracts obtained from subcellular organelles only high-molecular-weight acid phosphatase was detected, which is of lysosomal origin. Low-molecular-weight acid -phosphatase is restricted to the cell sap. Low- and high-molecular-weight acid phosphatases were characterized by their elution volumes, specific inhibition and activity with two substrates. It is suggested that the distribution pattern found om rat tissues could be common to all eukaryotic cells.
D000135:Acid Phosphatase / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D001921:Brain / Q000201:enzymology*; D007527:Isoenzymes / Q000378:metabolism; D007668:Kidney / Q000201:enzymology*; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D009928:Organ Specificity; D051381:Rats; D013347:Subcellular Fractions / Q000201:enzymology
D007527:Isoenzymes; D000135:Acid Phosphatase