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Equus przewalskii plasma protease inhibitor (Pi) system
Author(s) -
PATTERSON S. D.,
BELL K.,
MANTON V. J. A.
Publication year - 1990
Publication title -
animal genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.756
H-Index - 81
eISSN - 1365-2052
pISSN - 0268-9146
DOI - 10.1111/j.1365-2052.1990.tb03217.x
Subject(s) - biology , isoelectric focusing , trypsin , sialic acid , isoelectric point , protease , protease inhibitor (pharmacology) , biochemistry , locus (genetics) , pi , microbiology and biotechnology , enzyme , molecular mass , chymotrypsin , trypsin inhibitor , equus , genetics , gene , virus , viral load , antiretroviral therapy , zoology
Summary A detailed biochemical characterization of four of the five previously described alleles of the plasma protease inhibitor (Pi) system of Equus przewalskii was performed using both one‐ and two‐dimensional electrophoretic techniques. The proteins have been characterized in terms of isoelectric point, relative molecular mass, inhibitory activity to bovine trypsin and chymotrypsin, immunochemical cross‐reactivity, terminal sialic acid content and enzyme:inhibitor complex formation and the oxidation sensitivity of this interaction. Using these functional criteria, only three loci (Spi 1,2 and 3) were found to control the plasma Pi proteins of the E. przewalskii haplotypes. In contrast a fourth locus, Spi 4, was found in some E. caballus haplotypes. The significance of these results with respect to the complexity of the protein pattern exhibited by the equine Pi multigene family is discussed.