Phenothiazine binding by a homolog of calpactin, the pp60(src) tyrosine kinase substrage

K. L. Carraway, Y. Liu, D. Puett, K. L. Carraway, C. A C Carraway

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

Microvilli isolated from 13762 mammary ascites tumor cells contain a major calcium-sensitive protein (AMV-p35) that can be isolated with microvillar microfilament cores prepared by Triton X-100 extraction in the presence but not abscence of calcium. AMV-p35 can be readily purified from ethylene glycol bis(β-aminoethyl ether)-N,N,N',N'-tetraacetic acid extracts of the microfilament cores by chromatography on an anion exchange column, to which it does not bind. Immunoblot analysis indicates that AMV-p35 is related to calpactin I, the pp60(src) tyrosine kinase substrate. In the presence of calcium, AMV-p35 binds approximately 4 mol of chlorpromazine per mole of protein in a binding process showing apparent positive cooperativity, similar to calmodulin; however, in contrast to calmodulin, AMV-p35 also binds phenothiazine in the abscence of calcium.

Original languageEnglish (US)
Pages (from-to)46-50
Number of pages5
JournalFASEB Journal
Volume1
Issue number1
StatePublished - 1987
Externally publishedYes

ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Cell Biology

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