125I-insulin-like growth factor 1 was cross-linked to its receptor in human placenta microsomal membranes. The microsomes were treated with urea, with dithiothreitol or with both reagents prior to centrifugation at 100,000 × g. We found that >80% of the label was membrane-associated following separate treatment with urea or dithiothreitol, but >80% of the radio-activity remained in the supernatant after simultaneous exposure to both reagents. In identical experiments employing 125I-epidermal growth factor, no condition led to the release of >10% of label from the membrane. We conclude that the ligand binding subunit of the insulin-like growth factor 1 receptor, like peripheral membrane proteins, lacks a membrane anchoring domain.
|Number of pages||6|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Apr 14 1986|