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Animal blood groups and biochemical genetics1983; 14(2); 83-105; doi: 10.1111/j.1365-2052.1983.tb01065.x

Characterisation of the alpha 1-protease inhibitor system in Thoroughbred horse plasma by horizontal two-dimensional (ISO-DALT) electrophoresis. 1. Protein staining.

Abstract: The isoelectric points and the molecular weights of the major components of the eight Thoroughbred protease inhibitor (Pi) types have been determined by polyacrylamide gel isoelectric focusing and polyacrylamide gel pore gradient (ISO-DALT) electrophoresis respectively. The major Pi proteins focus in the range pH 3.74-4.43 and have molecular weights ranging from 55 000-72 000 daltons. Using the ISO-DALT method of electrophoresis, protein maps for the eight Thoroughbred Pi types have been presented for the first time. None of the homozygous Pi types are identical except for the types S1 and S2 which show partial identity. The results do not necessarily support Juneja et al.'s (1979) contention of two closely linked alpha 1 Pi systems based on molecular weight differences. It is suggested that the traditional nomenclature originally proposed by Braend (1970) be maintained to describe the eight Pi alleles in Thoroughbred horse plasma. The ISO-DALT method provides a sensitive technique which is superior to existing techniques for the analysis of the horse Pi system.
Publication Date: 1983-01-01 PubMed ID: 6193745DOI: 10.1111/j.1365-2052.1983.tb01065.xGoogle Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

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This research determines the characteristics of major components of eight Thoroughbred protease inhibitor (Pi) types, in particular their isoelectric points and molecular weights, using polyacrylamide gel isoelectric focusing and polyacrylamide gel pore gradient electrophoresis respectively. Contrary to previous research, it suggests that there are not two closely linked alpha 1 Pi systems based on molecular weight differences.

Major Points in the Study

  • The study investigates the alpha 1-protease inhibitor system in Thoroughbred horse plasma using a method of electrophoresis called ISO-DALT.
  • It focuses on the isoelectric points and the molecular weights of the major components of the eight Thoroughbred protease inhibitor types. These major components are found to focus in the range pH 3.74-4.43 and have molecular weights between 55 000-72 000 daltons.
  • According to the findings, none of the homozygous Pi types are identical except for the types S1 and S2, which display partial identity.

Interpretation of Findings

  • The data from this study does not support a previous contention by Juneja and colleagues (1979) that there are two closely linked alpha 1 Pi systems based on molecular weight differences.
  • Considering the implications of these results, the researchers suggest that the traditional nomenclature proposed by Braend in 1970 should continue to be used to describe the eight protease inhibitor (Pi) alleles in Thoroughbred horse plasma.

Advantages of the ISO-DALT Method

  • The ISO-DALT method of electrophoresis used in this study is highlighted as a superior technique for analyzing the horse protease inhibitor (Pi) system. The researchers attribute this advantage to its sensitivity compared to other existing techniques.

Cite This Article

APA
Pollitt CC, Bell K. (1983). Characterisation of the alpha 1-protease inhibitor system in Thoroughbred horse plasma by horizontal two-dimensional (ISO-DALT) electrophoresis. 1. Protein staining. Anim Blood Groups Biochem Genet, 14(2), 83-105. https://doi.org/10.1111/j.1365-2052.1983.tb01065.x

Publication

ISSN: 0003-3480
NlmUniqueID: 0263344
Country: Netherlands
Language: English
Volume: 14
Issue: 2
Pages: 83-105

Researcher Affiliations

Pollitt, C C
    Bell, K

      MeSH Terms

      • Animals
      • Blood Proteins / genetics
      • Blood Proteins / isolation & purification
      • Electrophoresis, Polyacrylamide Gel / instrumentation
      • Electrophoresis, Polyacrylamide Gel / methods
      • Horses / blood
      • Isoelectric Focusing / instrumentation
      • Isoelectric Focusing / methods
      • Molecular Weight
      • Protease Inhibitors / genetics
      • Staining and Labeling
      • alpha 1-Antitrypsin

      Citations

      This article has been cited 7 times.
      1. Samollow PB, Kammerer CM, Mahaney SM, Schneider JL, Westenberger SJ, VandeBerg JL, Robinson ES. First-generation linkage map of the gray, short-tailed opossum, Monodelphis domestica, reveals genome-wide reduction in female recombination rates. Genetics 2004 Jan;166(1):307-29.
        doi: 10.1534/genetics.166.1.307pubmed: 15020427google scholar: lookup
      2. Arthur H, Bell K, VandeBerg JL, van Oorschot RA. Plasma protease inhibitor (PI) system in the laboratory opossum, Monodelphis domestica. Biochem Genet 1996 Oct;34(9-10):389-99.
        doi: 10.1007/BF00554414pubmed: 8978911google scholar: lookup
      3. Patterson SD, Bell K. The equine protease inhibitory system (Pi): abnormal expressions of PiF, PiL, and PiS1. Biochem Genet 1986 Aug;24(7-8):529-43.
        doi: 10.1007/BF00504333pubmed: 3753429google scholar: lookup
      4. Milne EM. An improved method for the study of equine haptoglobin heterogeneity. Vet Res Commun 1990;14(6):433-9.
        doi: 10.1007/BF00367054pubmed: 2284705google scholar: lookup
      5. Potempa J, Wunderlich JK, Travis J. Comparative properties of three functionally different but structurally related serpin variants from horse plasma. Biochem J 1991 Mar 1;274 ( Pt 2)(Pt 2):465-71.
        doi: 10.1042/bj2740465pubmed: 2006910google scholar: lookup
      6. Patterson SD, Bell K, Shaw DC. The equine major plasma serpin multigene family: partial characterization including sequence of the reactive-site regions. Biochem Genet 1991 Oct;29(9-10):477-99.
        doi: 10.1007/BF02399689pubmed: 1772402google scholar: lookup
      7. Bell K, Arthur H, van Oorschot RA, VandeBerg JL. Antithrombin III (AT3) polymorphism in the marsupial Monodelphis domestica: identification and genetics. Biochem Genet 1992 Dec;30(11-12):591-601.
        pubmed: 1296573