A novel insulin-binding protein with a molecular weight of 30,000 daltons.
Analysis of mouse Swiss/3T3 fibroblasts and rat hepatoma H35 cells using the affinity cross-linking method revealed multiple forms of 125I-insulin binding components (Mr greater than 300,000) in the absence of reducing agents. The same analysis, in the presence of reducing agents, revealed two major components (Mr = 125,000 and Mr = 30,000). The Mr = 125,000 component appeared to be the alpha-subunit of the high-affinity insulin receptor, whereas the small insulin-binding component of Mr = 30,000 was not a degradation product of the alpha-subunit but was apparently associated with the insulin receptor. We suggest that it is likely a novel component for regulating the function of insulin receptor.
Shimizu
Y
Y
Department of Molecular and Cellular Biology, University of Arizona, Tucson 85721.
Shimizu
N
N
D000818:Animals; D002478:Cells, Cultured; D003432:Cross-Linking Reagents; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D005347:Fibroblasts / Q000032:analysis / Q000166:cytology / Q000648:ultrastructure; D007328:Insulin / Q000378:metabolism; D008114:Liver Neoplasms, Experimental / Q000032:analysis / Q000473:pathology / Q000648:ultrastructure; D051379:Mice; D008970:Molecular Weight; D051381:Rats; D011972:Receptor, Insulin / Q000032:analysis* / Q000378:metabolism; D014407:Tumor Cells, Cultured / Q000032:analysis / Q000473:pathology / Q000648:ultrastructure
D003432:Cross-Linking Reagents; D007328:Insulin; D011972:Receptor, Insulin