A p-nitrophenylphosphatase activity associated with the human erythrocyte membrane.
A p-nitrophenylphosphatase activity has been identified as a component of the human erythrocyte membrane. This activity is distinct from that associated with the cell's Na(+)+K(+)-dependent ATPase, Ca(2+)-dependent ATPase, or spectrin phosphatase. The activity described here is stimulated by Mn2+ but not by Ca2+ with or without calmodulin. A potential erythrocyte membrane substrate for this activity is a 95 kDa phosphoprotein that can be shown to undergo Mn(2+)-stimulated but not Mg(2+)-stimulated dephosphorylation.
Brissette
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RE
Department of Biochemistry and Molecular Biology, University of Medicine and Dentistry of New Jersey, New Jersey Medical School, Newark 07103-2714.
Swislocki
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Cunningham
E B
EB
D009597:4-Nitrophenylphosphatase / Q000097:blood*; D002147:Calmodulin / Q000494:pharmacology; D002413:Cations, Divalent / Q000494:pharmacology; D002469:Cell Separation; D002614:Chelating Agents / Q000494:pharmacology; D002845:Chromatography; D002850:Chromatography, Gel; D004910:Erythrocyte Membrane / Q000201:enzymology*; D006801:Humans; D008345:Manganese / Q000494:pharmacology; D010749:Phosphoprotein Phosphatases / Q000378:metabolism; D012685:Sepharose; D012995:Solubility; D013890:Thiourea / Q000494:pharmacology; D014909:Wheat Germ Agglutinins
D002147:Calmodulin; D002413:Cations, Divalent; D002614:Chelating Agents; D014909:Wheat Germ Agglutinins; D008345:Manganese; D012685:Sepharose; D010749:Phosphoprotein Phosphatases; D009597:4-Nitrophenylphosphatase; D013890:Thiourea