Improved procedure for purification of human platelet-derived growth factor.
نویسندگان
چکیده
منابع مشابه
Platelet-derived growth factor: purification and partial characterization.
A cationic protein that stimulates DNA synthesis in human cultured cells was isolated from human platelets by ion exchange chromatography, hydrophobic chromatography, gel chromatography, and gel electrophoresis in sodium dodecyl sulfate. The electrophoretic behavior of biologically active or radioiodinated and reduced growth factor indicated that the native protein (approximately 30,000 daltons...
متن کاملPlatelet-derived growth factor in human glioma.
Platelet-derived growth factor (PDGF) is a 30 kDa protein consisting of disulfide-bonded dimers of A- and B-chains. PDGF receptors are of two types, alpha- and beta-receptors, which are members of the protein-tyrosine kinase family of receptors. The receptors are activated by ligand-induced dimerization, whereby the receptors become phosphorylated on tyrosine residues. These form attachment sit...
متن کاملPlatelet-derived growth factor.
Platelet-derived growth factor was purified from fresh platelets by a large-scale procedure not involving the use of SDS (sodium dodecyl sulphate). The product, 0.5 mg of platelet-derived growth factor, obtained from about 3 x 1013 platelets migrated as a single component in analytical gel electrophoresis in the presence of SDS and showed no inhomogeneity on sedimentation-equilibrium analysis i...
متن کاملPurification of a membrane-derived human erythroid growth factor.
We have purified erythroid burst-promoting activity (BPA) from human lymphocyte plasma membranes by detergent extraction followed by gel-filtration, ion-exchange, and hydroxylapatite chromatography. BPA is a heat-stable integral membrane glycoprotein of Mr 28,000 by gel filtration whose activity is eluted from NaDodSO4/polyacrylamide gels as a broad band at Mr 25,000-29,000. The growth stimulat...
متن کاملPurification and analysis of proteinase-resistant mutants of recombinant platelet-derived growth factor-BB exhibiting improved biological activity.
Recombinant platelet-derived growth factor (PDGF)-BB was expressed and secreted from yeast in order to study the structure-function relationships of this mitogen. A simple purification scheme has been developed which yields greater than 95% pure PDGF-BB. Analysis of this recombinant PDGF-BB shows partial proteolysis after arginine-32. Substitution of this arginine residue, or arginine-28 [a pot...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Clinical Biochemistry and Nutrition
سال: 1989
ISSN: 1880-5086,0912-0009
DOI: 10.3164/jcbn.7.81