Journal article

ABSENCE OF COVALENT BINDING BY INSULIN TO ERYTHROCYTE AND RETICULOCYTE INSULIN-RECEPTORS

GM WARD, S CLARK, LC HARRISON

Biochemical and Biophysical Research Communications | ACADEMIC PRESS INC JNL-COMP SUBSCRIPTIONS | Published : 1984

Abstract

We investigated whether insulin forms covalent bonds with its receptors on erythrocytes and reticulocytes, as it does in adipocytes (1). Of the [125I]-insulin specifically bound at 37 degrees C to human and rat erythrocytes and rat reticulocytes, only 1.5-2.3% was non-dissociable on extensive washing. When ghosts prepared from the washed cells were solubilized in Triton X-100, only 0.6-1.5% of the specifically bound radioactivity appeared in the void volume of a Sephadex G-50 column. Moreover in contrast to adipocytes, this high molecular weight radioactivity was not immunoprecipitable by antibodies to the insulin receptor and was dissociated during chromatography in sodium dodecyl sulphate...

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