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

D. R. Marshak, D. M. Watterson, L. J. Van Eldik

Research output: Contribution to journalArticlepeer-review

97 Scopus citations

Abstract

We have purified the brain-specific 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.

Original languageEnglish (US)
Pages (from-to)6793-6797
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume78
Issue number11 II
DOIs
StatePublished - 1981

ASJC Scopus subject areas

  • General

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