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Abstract
We have characterized inter- and intrasubunit disulfide bonds of insulin receptors using reductant-treated rat liver and brain membranes. In autoradiograms of 125I-insulin cross-linked to both membranes pretreated with dithiothreitol, the intensity of affinity-labeled bands of the αβ-heterodimer and α-subunit was increased. Interestingly, labeled 120 and 110 kDa bands considered to be the α-subunit in partially reduced liver and brain membranes moved to 130 and 120 kDa bands under further reduced conditions, respectively. Double electrophoresis of each partially reduced band in the presence of reductants clearly demonstrates that the α-subunit of insulin receptors contains intrasubunit disulfide bonds.
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