Various electrophoretic techniques, immunoblotting and inhibitions of trypsin and chymotrypsin were used to study the variability of serum proteins in farmed red deer, Cervus elaphus L., of Czechoslovakian origin. Easily interpretable polymorphisms were observed in transferrin (variants A, B1, B2, C) and vitamin D binding protein, GC (variants D, F, I, S). Great variability was observed in the protease inhibitors PI2, PI3, PI4, PI5, and PI8 and in unidentified zones in the vicinity of albumin, but no genetical or physiological interpretation for this variability is yet available. Haemopexin, alpha 1 glycoprotein, protease inhibitors PI1, PI6 and PI7 were monomorphic.

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Summary A further α‐protease inhibitor system, PI4, was detected in porcine sera using either 2D agarose gel, pH 5.0‐PAGE, pH 9.0, or ID PAGE followed by immunoblotting with rabbit anti‐porcine PI2 or PI3 antisera. PI4 inhibited chymotrypsin, but not trypsin. Seven allelic variants of PI4 were described. By haplotyping of a‐protease inhibitor systems in 52 complete families it was shown that PI4 locus belongs to the PI gene cluster. The probable order of the PI loci was: PI1, PO1A, PI2, PI4, PI3.

Linkage relationships between A l B G , PGD, and HPX loci of rabbits were studied on segregation data in backcross matings. No sign of linkage between the three studied loci was found.