Title : Circular dichroism and fluorescence studies on interaction of calmodulin (CaM) with purified (Ca2(+)-Mg2+)ATPase of erythrocyte ghosts.

Pub. Date : 1990

PMID : 2150904






2 Functional Relationships(s)
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1 Moreover, quenching of the ATPase intrinsic fluorescence by acrylamide indicated that, depending on the enzyme conformational status, the accessibility of its tryptophan residues is influenced by direct interaction with CaM at micromolar Ca2+ concentration. Tryptophan dynein axonemal heavy chain 8 Homo sapiens
2 This was also confirmed by the observation that fluorescence energy transfer occurred from tryptophan residues of (Ca2(+)-Mg2+)ATPase to dansylated CaM. Tryptophan dynein axonemal heavy chain 8 Homo sapiens