Osmotic pressure measurements on insulin: anomalous results indicate that the monomer is preferentially adsorbed

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Monitoring Protein Adsorption with Solid-state Nanopores
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Monitoring Protein Adsorption with Solid-state Nanopores

Published on: December 2, 2011

P D Jeffrey

    Australian Journal of Biological Sciences
    |January 1, 1986
    PubMed

    The concentration dependence of the number average molecular weight of insulin at pH 2, ionic strength 0.05, and 20 degrees C as determined by osmotic pressure measurements indicates that the hormone is a homogeneous protein of molecular weight close to that of the dimer. Since sedimentation equilibrium experiments confirm what is well known, namely that insulin is a self-associating protein dissociating to monomer under these conditions, an explanation for the anomaly was sought in the possible loss of protein from solution by adsorption. Analysis of the results strongly supports this conclusion and consideration of the adsorption properties of insulin in terms of hydrophobic interactions shows them to be consistent with the behaviour of insulin as a self-associating protein. The monomer appears to be the primary molecular species responsible for insulin adsorption.

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