Hybrid protein containing heavy subunit of haptoglobin and light subunit of immunoglobulin G.

Abstract

Dimeric hybrid protein molecule consisting of disulfide-linked beta (heavy) subunit of haptoglobin (Hp) and L (light) subunit of immunoglobulin G, was synthesized. Molecular mass of the hybrid was 62.0 kd, sedimentation constant B20 = 2.43. Hemoglobin binding activity of the beta X L hybrid as compared with that of native Hp accounted for 25%. In immunological cross-reactivity the hybrid was found to be deficient in some antigenic determinants present in Hp and in Hp beta chain. Hybridization carried out in three-component mixtures (Hp beta subunits, Hp alpha (light) subunits, IgG-L) showed, that besides reconstituted tetramers of Hp (2 alpha X 2 beta) always the hybrid beta X L was formed, even at an excess of Hp alpha, an excess of IgG-L prevented the formation of tetrameric molecules. Conformational similarity of Hp alpha and IgG-L as disulfide linked with Hp beta is reflected in the interaction of respective conjugates with hemoglobin.

Cite this paper

@article{Osada1984HybridPC, title={Hybrid protein containing heavy subunit of haptoglobin and light subunit of immunoglobulin G.}, author={Jerzy Osada and Wanda Dobryszycka}, journal={Archivum immunologiae et therapiae experimentalis}, year={1984}, volume={32 2}, pages={221-9} }