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The Interaction between (Ca 2+ + Mg 2+ )‐ATPase and the Soluble Activator (Calmodulin) in Erythrocytes Containing Haemoglobin S
Author(s) -
Dixon Earl,
Winslow Robert M.
Publication year - 1981
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1981.tb02806.x
Subject(s) - calmodulin , enzyme , membrane , atpase , activator (genetics) , biochemistry , population , calcium , chemistry , biology , microbiology and biotechnology , receptor , medicine , environmental health , organic chemistry
S ummary . In normal erythrocytes, a membrane‐bound (Ca 2+ + Mg 2+ )‐ATPase is stimulated by a soluble activator, calmodulin. Since cells containing Hb S accumulate excessive Ca 2+ , the defect could lie in either the (Ca 2+ + Mg 2+ )‐ATPase or calmodulin. To decide between these two possibilities, we prepared (Ca 2+ + Mg 2+ )‐ATPase from erythrocytes of normal (AA), sickle cell trait (AS) and sickle cell disease (SS) individuals. Calmodulin was prepared from haemolysates from AA and SS erythrocytes. The enzyme prepared from SS ghosts had lower specific activity than that from AA membranes. Furthermore, calmodulin from either source did not stimulate the ATPase of SS erythrocytes. Enzyme from AS cells had specific activity similar to that of enzyme prepared from SS membranes. The enzymatic activity of a mixed cell population obtained from an SS patient 8 d following exchange‐transfusion was proportional to the per cent Hb A. These results indicate that calmodulin is unable to interact with the enzyme site on the SS membrane. This inability is believed to be due to a specific property of the membrane and not an abnormality of calmodulin itself.