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 language | English (US) |
|---|---|
| Pages (from-to) | 46-50 |
| Number of pages | 5 |
| Journal | FASEB Journal |
| Volume | 1 |
| Issue number | 1 |
| State | Published - 1987 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Agricultural and Biological Sciences (miscellaneous)
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Cell Biology
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Phenothiazine binding by a homolog of calpactin, the pp60(src) tyrosine kinase substrage. / Carraway, K. L.; Liu, Y.; Puett, D.; Carraway, K. L.; Carraway, C. A C.
In: FASEB Journal, Vol. 1, No. 1, 1987, p. 46-50.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Phenothiazine binding by a homolog of calpactin, the pp60(src) tyrosine kinase substrage
AU - Carraway, K. L.
AU - Liu, Y.
AU - Puett, D.
AU - Carraway, K. L.
AU - Carraway, C. A C
PY - 1987
Y1 - 1987
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0023546914&partnerID=8YFLogxK
M3 - Article
C2 - 3301497
AN - SCOPUS:0023546914
VL - 1
SP - 46
EP - 50
JO - FASEB Journal
JF - FASEB Journal
SN - 0892-6638
IS - 1
ER -