Characterization of acid phosphatase isoenzymes in human skin fibroblasts.
The multiple acid phosphatase isoenzymes of cultivated skin fibroblasts were investigated in an effort to further clarify the basis of the observed molecular heterogeneity. Treatment with neuraminidase did not alter the migration of isoenzymes present prior to treatment with neuraminidase did not alter the migration of isoenzymes present prior to treatment, but additional isoenzymes were detectable after treatment. Variation of enzymes, permitting prediction of net charge and molecular size differences. Isoelectric focusing between pH 5.0 and pH 8.0 demonstrated three isoenzymes of acid phosphatase in the total cell homogenate and in the lysosomal fraction, two of which appeared to have similar isoelectric points.
D000135:Acid Phosphatase / Q000378:metabolism*; D002478:Cells, Cultured; D005347:Fibroblasts / Q000201:enzymology; D006801:Humans; D007525:Isoelectric Focusing; D007527:Isoenzymes / Q000378:metabolism*; D008247:Lysosomes / Q000201:enzymology; D012867:Skin / Q000201:enzymology*; D013347:Subcellular Fractions / Q000201:enzymology
D007527:Isoenzymes; D000135:Acid Phosphatase