Negative and positive site-site interactions, and their modulation by pH, insulin analogs, and monoclonal antibodies, are preserved in the purified insulin receptor.
The kinetic properties of the insulin receptor were studied in solution after its purification to homogeneity. Dissociation of 125I-labeled insulin at a 1:50 dilution was not first order; unlabeled insulin at physiological concentrations accelerated the dissociation rate with a maximal effect at app...
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| Pubblicato in: | Proc Natl Acad Sci U S A |
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| Autori principali: | , , , , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
National Academy of Sciences
1988
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC282465/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/3054887/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.85.22.8400 |
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