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This report describes the partial purification and characterization of mammary stimulating factor (MSF), a mitogenic peptide isolated from serum which initiates growth in mouse mammary epithelium. By using ion-exchange chromatography, gel filtration, and isoelectric focusing, MSF was purified 250-fold from porcine serum. It is a heat-stable protein of molecular weight 10,100--10,400 with an isoelectric point of 5.5--6.0. MSF initiates DNA synthesis in vitro in mammary epithelium to a greater extent than in mouse mammary tumor cells (CZF), 3T3 cells, or chick embryo cells. Comparison of the biological, physical, and immunological properties of MSF with other established growth-promoting peptides suggests that MSF is a unique serum factor.
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Ptashne et al. (1979) studied this question.
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