Abstract
To understand the biology and the biochemistry of the epidermal growth factor (EGF) precursor in normal tissues we partially purified the EGF precursor from mouse kidney. The precursor was purified by affinity chromatography, using wheat germ lectin and antibodies to murine EGF. The EGF precursor is a glycosylated integral membrane protein of apparent molecular mass of 140-150 kDa. The solubilized EGF precursor is biologically active as evidenced by its ability to compete with 125I-labeled EGF for binding to the EGF receptor in intact fibroblasts and its ability to stimulate the growth of cells dependent on EGF for growth. The EGF precursor from mouse kidney can be proteolytically processed by the EGF-associated arginine esterase into a smaller fragment (97 kDa) that retains both immunologic sensitivity to EGF antiserum and biological activity. Extensive digestion of the EGF precursor with pepsin liberates a biologically and immunologically active protein of approximately the size of mature EGF.
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