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A p‐nitrophenylphosphatase activity associated with the human erythrocyte membrane
Author(s) -
Brissette Renee E.,
Swislocki Norbert I.,
Cunningham Earlene Brown
Publication year - 1991
Publication title -
american journal of hematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.456
H-Index - 105
eISSN - 1096-8652
pISSN - 0361-8609
DOI - 10.1002/ajh.2830380303
Subject(s) - dephosphorylation , spectrin , phosphoprotein , phosphatase , erythrocyte membrane , membrane , atpase , calmodulin , biochemistry , chemistry , red blood cell , ouabain , substrate (aquarium) , microbiology and biotechnology , biophysics , phosphorylation , biology , cell , enzyme , cytoskeleton , sodium , ecology , organic chemistry
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 Mn 2+ but not by Ca 2+ 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.