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. 1981 Nov;78(11):6793–6797. doi: 10.1073/pnas.78.11.6793

Calcium-dependent interaction of S100b, troponin C, and calmodulin with an immobilized phenothiazine.

D R Marshak, D M Watterson, L J Van Eldik
PMCID: PMC349137  PMID: 6947252

Abstract

We have purified the brain-specific protein S100b by affinity-based adsorption chromatography on phenothiazine-Sepharose conjugates and studied the interaction of this and other calcium-modulated proteins with the immobilized antipsychotic drug. Bovine brain calmodulin, rabbit skeletal muscle troponin C, and bovine brain S100b bind to phenothiazine-Sepharose in a calcium-dependent manner. These three proteins competitively inhibit the calcium-dependent binding of 125I-labeled chicken gizzard calmodulin to the immobilized drug. However, carp parvalbumin and chicken intestinal vitamin D-dependent calcium binding protein do not inhibit the phenothiazine--calmodulin interaction. These results suggest that the known amino acid sequence homology among calmodulin, troponin C, and S100b may be reflected in a similar functional domain present in these proteins but absent in parvalbumin and vitamin D-dependent protein.

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Selected References

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