Characterization of Fe2+-activated acid phosphatase in rat epidermis.
A particulate acid phosphatase (EC 3.1.3.2, orthophosphoric monoester phosphohydrolase (acid optimum)) was extracted in 1 M KCl, from 2-day rat epidermis. The enzyme has a Mr of 32,000, but two forms, F1 and F2 with pI values of 8.6 and 8.3, respectively, were identified while the pI values of other acid phosphatases soluble in sucrose and Triton X-100 were all acidic. F1 and F2 also differed from other epidermal acid phosphatases because they were (a) activated by Fe2+ and reducing agents, (b) showed immunological cross-reactivity with purple acid phosphatase of rat spleen and (c) dephosphorylated phosvitin and alpha-casein even though they had rather high Km values.
D000135:Acid Phosphatase / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D000831:Animals, Newborn; D001205:Ascorbic Acid / Q000494:pharmacology; D004789:Enzyme Activation; D005260:Female; D005779:Immunodiffusion; D007501:Iron / Q000494:pharmacology*; D007700:Kinetics; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains; D012867:Skin / Q000201:enzymology*; D013379:Substrate Specificity
D007501:Iron; D000135:Acid Phosphatase; D001205:Ascorbic Acid