Dietrich Brandenburg

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X-ray analysis, circular dichroism, receptor binding and biological potencies of chemically modified insulins suggest that the conformation of the insulin molecule is critical to the formation of both the zinc insulin hexamer and the insulin-receptor complex. Results are consistent with an insulin receptor-binding region including many of the hydrophobic(More)
Starting with the epoch-making discovery of proinsulin, C-peptide has played an important interdisciplinary role, both as part of the single-chain precursor molecule and as an individual entity. In the pioneering years, fundamental systematic experiments unravelled new biochemical mechanisms and chemical structures. After the first detection of C-peptide in(More)
There is morphological and biochemical evidence that insulin is internalized in hepatocytes. The present study was designed to investigate the fate of the insulin receptor itself, subsequently to the initial binding step of the hormone to the hepatocyte plasma membrane. The insulin receptor was labeled with a 125I-photoreactive insulin analogue(More)
Previous studies have demonstrated differences in the size of insulin receptor subunits in brain and adipocytes that appear to involve variations in glycosylation of the proteins. In this report, we examined the degree of homology in the protein backbones of insulin receptors in both tissues by peptide mapping and compared the mRNAs encoding the receptors(More)
The first step of insulin's many cellular functions is specific binding to receptors on the plasma membrane of target cells. The subsequent molecular basis of insulin action, particularly the coupling mechanism(s) involved in transmitting the biological message, remains largely unknown. Our approach to the problem centres on the application of a series of(More)
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