Modulation of human erythrocyte Ca2+/Mg2+ ATPase activity by phospholipase A2 and proteases. A comparison with calmodulin |
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Authors: | R D Taverna D J Hanahan |
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Affiliation: | Department of Biochemistry The University of Texas Health Science Center San Antonio, Texas 78284 USA |
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Abstract: | The human erythrocyte membrane ATPase responded to the presence of an acidic phospholipase A2 and to low levels of trypsin (and chymotrypsin) in much the same way as it did to calmodulin isolated from human erythrocytes. The increased concentration of ATP hydrolyzed in 1 hour was similar to that observed when calmodulin had been added to a suspension of membranes during the assay. The observations reported here strongly suggest that activation of the ATPase can proceed by introducing apparently distinct perturbations either to the protein or to phospholipid domains of the erythrocyte membrane. |
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Keywords: | BHT 2 6 ditert butyl 4 methylphenol DEGS diethylglycol succinate NPGB p-nitrophenyl-p′-guanidino benzoate |
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