Abstract:
:IGF-I receptors were partially purified from red and white skeletal muscle by lectin-affinity chromatography and the resultant fraction was depleted of insulin receptors by insulin affinity chromatography. Equilibrium binding of 125I-IGF-I to receptor preparations from red and white muscle yielded identical Scatchard plots. The integrity of the IGF-I receptor preparation in the two fiber types was identical as determined by affinity cross-linking. The tyrosine kinase activity of the receptor from red muscle was 2-3-fold more active towards exogenous substrates in both the basal and ligand-activated states as compared to white muscle. These data show that there is IGF-I-dependent kinase activity intrinsic to IGF-I receptors from skeletal muscle, and suggest that identical cellular factors may regulate the kinase activity of insulin and IGF-I receptors in a parallel manner in vivo.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Zorzano A,James DE,Ruderman NB,Pilch PFdoi
10.1016/0014-5793(88)80093-0subject
Has Abstractpub_date
1988-07-18 00:00:00pages
257-62issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(88)80093-0journal_volume
234pub_type
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