PARTIAL-PURIFICATION AND CHARACTERIZATION OF MAMMARY STIMULATING FACTOR, A PROTEIN WHICH PROMOTES PROLIFERATION OF MAMMARY EPITHELIUM

被引：24

作者：

PTASHNE, K ^{[1
]}

HSUEH, HW ^{[1
]}

STOCKDALE, FE ^{[1
]}

机构：

[1] STANFORD UNIV,SCH MED,DEPT BIOL SCI,STANFORD,CA 94305

来源：

BIOCHEMISTRY | 1979年 / 18卷 / 16期

关键词：

D O I：

10.1021/bi00583a015

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 10100-10400 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. © 1979, American Chemical Society. All rights reserved.

引用

页码：3533 / 3539

页数：7

共 30 条

[1] RADIOIMMUNOASSAY OF A HUMAN-SERUM GROWTH-FACTOR FOR BALB-C-3T3 CELLS - DERIVATION FROM PLATELETS [J].