Calcium-dependent interaction of S100b, troponin C, and calmodulin with an immobilized phenothiazine.
- 1 November 1981
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 78 (11), 6793-6797
- https://doi.org/10.1073/pnas.78.11.6793
Abstract
The brain-specific protein S100b was purified from bovine brain by affinity-based adsorption chromatography on phenothiazine-Sepharose conjugates and studied the interaction of this and other Ca-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 Ca-dependent manner. These 3 proteins competitively inhibit the Ca-dependent binding of 125I-labeled chicken gizzard calmodulin to the immobilized drug. Carp parvalbumin and chicken intestinal vitamin D-dependent Ca binding protein do not inhibit the phenothiazine-calmodulin interaction. 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.This publication has 37 references indexed in Scilit:
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