作者: King L , Cohen S , Carpenter G
DOI:
关键词: Biochemistry 、 Epidermal growth factor 、 Membrane protein 、 Proto-oncogene tyrosine-protein kinase Src 、 Protein kinase A 、 Phosphorylation 、 Epidermoid carcinoma 、 TGF alpha 、 Chemistry 、 Platelet-derived growth factor receptor
摘要: Membranes prepared from A-431 human epidermoid carcinoma cells retained the ability to bind 125I-labeled epidermal growth factor (EGF) in a specific manner. In presence of [gamma-32]ATP and Mn2+ or Mg2+, this membrane preparation was capable phosphorylating endogenous proteins, as well exogenously added histone. The binding EGF membranes vitro resulted several-fold stimulation phosphorylation reaction. reaction not dependent on cyclic AMP GMP. These findings suggest that one biochemical consequences is rapid activation AMP-independent system. membrane-associated protein kinase by appears be reversible phenomenon. could solubilized number non-ionic detergents with retention both activity EGF-enhanced proteins. purified affinity chromatography. EGF-binding activity. Analysis affinity-purified SDS gel electrophoresis indicated major band molecular weight 150,000 several trace bands. evidence suggests receptor for substrate co-purification EGF-stimulated an inherent close relationship. tyrosine residues regard resembles src kinase.