[Initial treatment of type I diabetes mellitus with biosynthetic human insulin].
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Biomedical subjects
Publications and source records attributed to S Steinhilber.
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Guinea-pig antisera to bovine insulin and proinsulin were analysed and the association constants and the concentrations of combining sites specific for insulin and for the C-chain were determined. Both antisera contained combining sites with higher (Ak(1) sites) and lower (Ak(2) sites) affinities for the cross-reacting antigens.Antisera produced in response to both insulin and proinsulin had similar concentrations of both the more affine and less affine insulin-specific binding sites. Bovine insulin contaminated with traces of proinsulin did not induce antibodies specific for the C-chain.Antisera to proinsulin contained equal amounts of high affinity binding sites specific for the C-chain and for the insulin part of the molecule. After absorption of the insulin-specific antibodies these sera can be used for the immunoassay of proinsulin.
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The binding of biosynthetic human insulin (BHI) and pork insulin to anti-pork insulin antibodies was tested at an insulin concentration of 4 microunits/ml. Identical binding data were obtained. The binding of the two insulins to mononuclear lymphocytes was also identical. The data are compared to previous results obtained with synthetic human insulin. Previously, we investigated the in vitro properties of fully synthetic human insulin from Dr. Rittel, Ciba-Geigy, Basel. Receptor binding of this human insulin was identical to pork insulin. The binding properties of the new BHI from Lilly (Indianapolis) were studied with human antibodies and freshly isolated human monocytes.