Zur Strukturregel der Antikörper. Die Primärstruktur eines monoklonalen IgG1-Immunglobulins (Myelomprotein Nie), I. Reinigung und Charakterisierung des Proteins, der L- und H-Ketten, der Bromcyanspaltprodukte und der Disulfidbrücken

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Abstract
Myeloma protein Nie was isolated from the serum of a myeloma patient by free flow continuous high voltage electrophoresis or by Pevicon-block electrophoresis. It was further purified by ion-exchange chromatography and gel filtration, and characterized by amino acid analysis and end group determination. Serologically the protein belongs to the Ig[immunoglobulin]G1 subclass. It was typed as Gm1+, 2-, 4- and 17+. The L-chain is of the .kappa. type. The L- and H-chains were separated by gel-filtration after partial reduction and alkylation and characterized by amino acid analysis and end group determination. The F(ab)- and Fc-fragments, prepared by limited tryptic digestion, were separated and characterized. CNBr splitting products were prepared from the intact IgG and from the Fc- and the partially reduced and alkylated F(ab)-fragment. These splitting products were purified and characterized by amino acid analysis and end group determination. By means of these CNBr splitting products and by partial reduction and alkylation, the disulfide bridges in the protein could be localized: 1 L-H-bridge, 2 inter-H-bridges and 4 loop forming intra-H-bridges.

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