ISO-DALT characterization of 12 'new' equine plasma protease inhibitor (Pi) alleles.
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.
Patterson
S D
SD
Department of Physiology and Pharmacology, University of Queensland, St Lucia, Australia.
Bell
K
K
D000483:Alleles; D000818:Animals; D002918:Chymotrypsin / Q000097:blood; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D006736:Horses / Q000235:genetics*; D007525:Isoelectric Focusing / Q000379:methods; D008970:Molecular Weight; D011480:Protease Inhibitors / Q000097:blood / Q000235:genetics*; D014361:Trypsin Inhibitors / Q000097:blood / Q000235:genetics
D011480:Protease Inhibitors; D014361:Trypsin Inhibitors; D002918:Chymotrypsin