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 residues important to dimerisation in addition to more polar surface residues. There is a further possibility of formation of an antiparallel sheet structure between the insulin and receptor molecules in the complex similar to that between monomers in the insulin dimer.

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Prof. Dr. tlerman Mark zum 80. Geburtstag gewidmet (Einpangsdatum: 31. Oktober 1974) ZUSAM M FNFASSIJNG : Das nach Geiger durch selektive Hutyloxycarbonylierung von Insulin lcicht zugiingliche l\f 2 4 1 .NCH 29-Bis( ror-butyloxycarbonyl)insulin wurdc chromatographisch gercinigt und als Aminokomponente fur Peptidsynthesen mit aktiven Estern von rr.rr-Butyloxycarbonql-geschutztcn Aminosiiuren cingesetzt. Auf dicse Wcise gelang die Partialsynthese von itzB'-Lcucyl-. (;lycyl-. Lysyl-und Glutamylinsulin. Die clektrophoretisch (pH 2 und 8.6) und dunnschichtromatofraphisch einheitlichen Analoga wurden durch biologische, immunologische und C'D-spcktralc Datcn charaktcrisiert und konnten kristallisicrt werden. SUMMARY:,v,\l , ,ycH>''-Bis( rPrr-butyloxycarbony1)insulin. easily obtaincd by selective butyloxycarbonylation of insulin according to Gcigcr. was purificd by chromatography and applied as amino component for peptidc synthcscs with active esters of amino acids protected by thc butyloxycarbonyl group. By this method the partial synthesis of A""'-lcucyl-. glycyl-, lysyl-, and glutamylinsulin was achieved. The analogues showing homogeneity in electrophoresis (pH 2 and 8.6) and thin layer chromatography. wcrc charactcrired by biological. immunological. and CD-spectral data and could be crystallired.

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