Title : Regulation of the erythrocyte Ca(2+)-ATPase at high pH.

Pub. Date : 1994 Mar 15

PMID : 8143719






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 The maximal velocity at high pH becomes insensitive to both calmodulin and controlled proteolysis, although calmodulin binds to the protein with similar affinities at pH 7.0 and 8.0, as indicated by similarity in binding to a calmodulin-Sepharose resin and in dependence on calmodulin concentrations when the pH is increased. Sepharose calmodulin 1 Homo sapiens
2 The maximal velocity at high pH becomes insensitive to both calmodulin and controlled proteolysis, although calmodulin binds to the protein with similar affinities at pH 7.0 and 8.0, as indicated by similarity in binding to a calmodulin-Sepharose resin and in dependence on calmodulin concentrations when the pH is increased. Sepharose calmodulin 1 Homo sapiens
3 The maximal velocity at high pH becomes insensitive to both calmodulin and controlled proteolysis, although calmodulin binds to the protein with similar affinities at pH 7.0 and 8.0, as indicated by similarity in binding to a calmodulin-Sepharose resin and in dependence on calmodulin concentrations when the pH is increased. Sepharose calmodulin 1 Homo sapiens