Intermediates in the reassociation of reduced haptoglobin.
Oxidative reassociation of alpha and beta subunits of human and equine haptoglobins as well as of two 2 alpha . 2 beta tetrameric hybrids made of subunits of each haptoglobin was studied following reduction of interchain disulphide bridges and also with isolated, PHMB-protected subunits in homologous and heterologous systems. Molecular mass and subunit composition of the intermediates appearing in the process of successive oxidation of -SH groups were determined by SDS-polyacrylamide-gel electrophoresis. The yield of subunit reassociation into homologous and heterologous tetramers 2 alpha . 2 beta was very high (75-80%) and the reassociated haptoglobins exhibited properties of native proteins in binding reactions with haemoglobin and with specific antibodies.
D000818:Animals; D006242:Haptoglobins / Q000032:analysis* / Q000276:immunology; D006736:Horses / Q000276:immunology; D006801:Humans; D007700:Kinetics; D008970:Molecular Weight; D010084:Oxidation-Reduction; D010446:Peptide Fragments; D010544:Peroxidases / Q000378:metabolism; D055503:Protein Multimerization; D011817:Rabbits / Q000276:immunology
D006242:Haptoglobins; D010446:Peptide Fragments; D010544:Peroxidases