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Phenothiazine binding by a homolog of calpactin, the pp60 src tyrosine kinase substrate
Author(s) -
Iii Kermit L. Carraway,
Liu Yuecheung,
Puett David,
Carraway Kermit L.,
Carraway Coralie A. Carothers
Publication year - 1987
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.1.1.3301497
Subject(s) - calmodulin , chemistry , biochemistry , microfilament , calcium , tyrosine kinase , tyrosine , calmodulin binding proteins , microbiology and biotechnology , stereochemistry , biophysics , biology , enzyme , signal transduction , cytoskeleton , organic chemistry , cell
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 absence 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 absence of calcium.—C arraway , K. L., III; L iu , Y.; P uett , D; C arraway , K. L.; C arothers C arraway , C. A. Phenothiazine binding by a homolog of calpactin, the pp60 src tyrosine kinase substrate. FASEB J. 1: 46‐50; 1987.