Abstract
Twelve equine protease inhibitory alleles, PiE,H,J,K,L2,O,P,Q,R,V,X,Z, have been characterized in terms of isoelectric point, molecular mass and inhibitory activity to bovine trypsin and chymotrypsin by ISO-DALT electrophoresis. Protein maps for 20 Pi alleles including those of the eight ''Thoroughbred'' alleles (PiF,G,I,L,N,S1,S2,U) have now been determined. Five pairs of alleles,S1/S2,G/K,L/L2, P/R and U/Z, possessed varying numbers of common proteins ranging from one protein in the case of G/K and L/L2 to six in the case of U/Z. Based on these results and studies of the abnormal expressions of PiF, PiL and PiS1, a theory of at least three closely linked loci has been postulated to account for the marked heterogeneity of the equine protease inhibitory system.

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