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Endocrinology, Vol 113, 415-417, Copyright © 1983 by Endocrine Society


ARTICLES

Purification of an estrogen-regulated breast cancer protein by monoclonal antibody affinity chromatography

DJ Adams, H Hajj, KG Bitar, DP Edwards and WL McGuire

An estrogen-regulated cytoplasmic protein has been purified from MCF-7 human breast cancer cells with anion exchange and monoclonal antibody affinity chromatographies. The purified protein has a monomeric mol wt of 28,000 and isoelectric species with pI's between 5.9 and 6.0. Amino acid analysis indicates the protein is acidic, is probably hydrophilic, and contains unusually low amounts of methionine and half cystine. This rapid, two-step procedure produces purified protein in high yield and demonstrates the power of monoclonal antibodies in protein purification.


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J. G. Kiang, I. D. Gist, and G. C. Tsokos
Cytoprotection and regulation of heat shock proteins induced by heat shock in human breast cancer T47-D cells: role of [Ca2+]i and protein kinases
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[Abstract] [Full Text]


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D. Ciocca and M. Dufau
Estrogen-dependent Leydig cell protein recognized by monoclonal antibody to MCF-7 cell line
Science, October 26, 1984; 226(4673): 445 - 446.
[Abstract] [PDF]




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Copyright © 1983 by The Endocrine Society