Characterization of skeletal muscle insulin receptor.

Abstract:

:The insulin receptor from rat skeletal muscle was characterized. Treatment of muscle membranes with the photoactive insulin analog, 125I[N-epsilonB29-monoazidobenzoyl]-insulin revealed a single protein band of 135,000 Da, the alpha subunit. Iodination of total membrane protein followed by Triton X-100 solubilization and immunoprecipitation demonstrated the presence of a protein band of 90,000 Da, the beta subunit, together with a protein band of 190,000 Da, which may be the receptor precursor. In partially purified receptor preparations, the beta subunit exhibited dose-dependent, insulin-stimulated phosphorylation with incorporation of phosphate solely into tyrosine residues, which was also observed in the 190,000-Da receptor precursor. Purified plasma membranes contained a large amount of insulin-degrading activity which had to be inactivated prior to performing insulin-binding studies. If degradation of insulin was not prevented, apparent enhanced binding in the presence of unlabeled insulin was observed.

journal_name

Arch Biochem Biophys

authors

Dubler RE,Whipple JH,Larner J

doi

10.1016/0003-9861(85)90611-3

subject

Has Abstract

pub_date

1985-01-01 00:00:00

pages

119-29

issue

1

eissn

0003-9861

issn

1096-0384

pii

0003-9861(85)90611-3

journal_volume

236

pub_type

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