ISSN:
1573-4927
Keywords:
serpin
;
Equus caballus
;
two-dimensional electrophoresis
;
protein blotting
;
pulsed liquid phase sequencing
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Abstract The equine Pi system, which is highly polymorphic and was considered to be controlled by a single locus, has been shown to be controlled by four loci (namedSpi 1–4). This system is the equine equivalent of the major human plasma serpin (serine protease inhibitor), human α1PI. Twenty-two haplotypes of the equine Pi system have been characterized by two-dimensional electrophoresis, resulting in the assignment of pI,M r, and bovine trypsin and chymotrypsin inhibition characteristics to 109 proteins. These proteins have been analyzed further to determine their relatedness to each other as well as to human α1PI using immunochemical, structural, and functional criteria. The amino acid sequences of the N termini and reactive-site regions have been determined on proteins from each of the four equineSpi loci. This allowed the designation of the proteins from theSpi 1 locus as being METserpins and the functional equivalents of human α1PI. TheSpi 4 proteins are ARGserpins, and by alignment theSpi 2 proteins are ILEserpins, the first so far described. The P1 residue for theSpi 3 proteins was unable to be determined. The limited peptide and immunopeptide mapping revealed that proteins from all four loci were closely related, but within the four there were two pairs (Spi 1 and2 andSpi 3 and4) which were more related. All were probably derived from the same gene that gave rise to human α1PI.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00554047
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