Previous studies on the amino acid sequences and on the amino acid composition of peptides revealed genetic polymorphism both of the haemoglobin alpha-chain (Hb alpha) and beta-chain (Hb beta) in rabbits. In this study, rabbit haemolysates were analysed by isoelectric focusing in a narrow pH range (6.7-7.7) and by reversed-phase chromatography. Two variants were found for both Hb alpha and Hb beta. The two methods detected the same variants in this material. Inheritance data were consistent with the hypothesis that the observed Hb alpha and Hb beta variants were each controlled by two codominant, autosomal alleles. Haemoglobin polymorphism appears to be frequent in domestic rabbits since both variants of each chain were observed in all the three breeds studied.
By comparing electrophoretic patterns of urinary proteins from males of different inbred strains and pertinent hybrids, a new polymorphic locus designated Mur-2 has been detected.
In an electrophoretic analysis of 198 milk samples from the Massa and Biella breeds of sheep, six different alpha s-casein phenotypes were observed, of which three have not been reported previously.
A monoclonal antibody termed B2 Val 7C7, was produced by the fusion of xenoimmune mouse spleen cells with Sp2/0.Ag 14 myeloma cells. This antibody is specific for a polymorphic lymphocyte antigen; it was detected on cells from 138 out of 177 cattle by both 125I-labelled protein A (solid-phase radioimmunoassay, SPRIA) and gold-labelled protein A (immunogold). Its binding was tested on various cell types (peripheral blood lymphocytes, monocytes, polymorphonuclear cells (PMN), thymocytes) from a variety of normal bovine donors. On the one hand, B2 Val 7C7 detects a determinant present on all IgG-bearing lymphocytes, on 20% of the non-IgG-bearing lymphocytes and on the majority of the monocytes. On the other hand, no binding occurs on any PMN or thymocytes. The detected membrane antigen was isolated by immunoprecipitation from an NP 40 extract of 3H-leucine-labelled cells. On SDS-PAGE, it appears to be composed of two sub-units: a 32 000-dalton and a 27 000-dalton chain. These results show that B2 Val 7C7 recognizes an alloantigenic specificity present on an Ia-like antigen.