Heparin-binding Properties of Human Serum Spreading Factor*

作者: D W Barnes , J E Reing , B Amos

DOI: 10.1016/S0021-9258(17)39338-9

关键词: Ionic strengthPlasma protein bindingBiological activityCell cultureBiologyBiochemistryHeparinUreaGlycoproteinVitronectin

摘要: Human serum spreading factor (SF) is a blood glycoprotein that promotes attachment and influences growth, migration, differentiation of variety animal cells in culture. SF purified from human plasma or by chromatographic methods reported previously (Barnes, D. W., Silnutzer, J. (1983) Biol. Chem. 258, 12548-12552) does not bind to heparin-Sepharose under conditions physiological ionic strength pH. In further examination the heparin-binding properties SF, we found exposure 8 M urea altered several protein, including heparin affinity, these alterations remained after removal solutions. Urea-treated bound conditions, salt concentrations 0.4 higher were required for elution urea-treated at pH 7.0. The alteration also was observed upon protein heat acid. Treatment with urea, heat, acid resulted additionally greatly decreased cell spreading-promoting activity molecule. biological associated reduced ability treated culture substratum, prerequisite attachment-promoting Experiments examining native unfractionated indicated major portion did

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