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Home / Equine Research Bank / Acta Vet Scand / Identification of the PR prealbumin proteins in horse serum.
Acta veterinaria Scandinavica1977; 18(4); 458-470; doi: 10.1186/BF03548409

Identification of the PR prealbumin proteins in horse serum.

Abstract: The Pr protein, which is one of the major equine acidic prealbumins and which consists of a large number of phenotypes, has been studied with regard to its chemical identity. Serum samples of known Pr phenotype which had been treated with varying amounts of bovine trypsin were subjected to starch gel electrophoresis at pH 4.8. When a certain amount of trypsin was used, the Pr protein was markedly affected, whereas the other acidic prealbumins retained their normal electrophoreitic pattern. Extracts from three different regions of the acidic prealbumin field were tested by the casein precipitating inhibition test (CPI-test). Marked antitrypsin effect appeared against the extract from the Pr zone but not against the extracts from the two other acidic prealbumin zones. When acidic starch gel electrophoresis was combined with the CPI-test, a broad inhibitory zone appeared in the area of the Pr proteins. Pr protein was isolated by the use of agarose gel electrophoresis and sepharose column chromatography. The isolated protein which was tested for purity by gel electrophoresis had a molecular weight of about 60,000. It is concluded that the equine Pr protein corresponds to αi-antitrypsin. Pr-proteinet er et av de fremtredende proteiner i gruppen sure prealbuminer i hesteserum og har et stort antall fenotyper. Proteinet er undersøkt med henblikk på dets kjemiske identitet. Serumprøver av en kjent Pr-fenotype som var blitt behandlet med varierende mengder med bovint trypsin, ble kjørt på stivelsesgelelektroforese ved pH 4.8. Ved tilsetning av en bestemt mengde trypsin, ble det en tydelig påvirkning på Pr-proteinene, mens de øvrige sure prealbuminer beholdt sitt normale elektroforesemønster. Ekstrakter fra tre forskjellige soner av feltet med de sure prealbuminer ble testet ved hjelp av casein precipitation inhibition test (CPI-test). En tydelig antitrypsinvirkning viste seg mot ekstraktet fra Pr-sonen, derimot var det ingen reaksjon mot ekstraktene fra de to øvrige prealbuminsoner. Ved bruk av elektroforese på sur stivelsesgel kombinert med CPI-test fremkom en bred hemningssone i Pr-proteinenes område. Pr-protein ble isolert ved hjelp av elektroforese på agarosegel og sepharose-kromatografi. Renheten av det isolerte protein som hadde en molekylvekt på omkring 60 000, ble testet ved hjelp av gelelektroforese. Det konkluderes med at Pr-proteinet i hesteserum tilsvarer α-anti-trypsin.
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Publication Date: 1977-01-01 PubMed ID: 596326PubMed Central: PMC8377659DOI: 10.1186/BF03548409Google Scholar: Lookup
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  • Journal Article

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research article investigates the nature of the ‘Pr’ protein, one of the major acidic prealbumins in horse serum, concluding that this protein corresponds to alpha-1-antitrypsin.

Research Objective and Methodology

  • The primary objective of this research was to comprehend the chemical identity of the Pr protein, a significant acidic prealbumin in horse serum.
  • For this, serum samples with known Pr phenotypes were treated with different amounts of bovine trypsin and then subjected to starch gel electrophoresis at a pH of 4.8.
  • The influence on the Pr protein became evident after a precise quantity of trypsin was added, highlighting a difference compared to other acidic prealbumins that maintained their standard electrophoretic pattern.

Use of Casein Precipitating Inhibition Test (CPI-test)

  • The Casein Precipitating Inhibition Test (CPI-test), which examines the anti-tryptic activities of extracts, was used after extracting from three different regions of the acidic prealbumin field.
  • This test showed a prominent anti-trypsin effect against an extract from the Pr protein zone, but not against the others.
  • Combining the CPI-test with starch gel electrophoresis resulted in a broad inhibitory zone in the Pr protein region.

Isolation and Identification of Pr protein

  • Pr protein was isolated using agarose gel electrophoresis and sepharose column chromatography.
  • The purity of this isolated protein, which had a molecular weight of about 60,000, was tested using gel electrophoresis.
  • The research concluded that the Pr protein in horse serum equates to the alpha-1-antitrypsin.

Key Findings and Conclusion

  • The experimentation enabled the researchers to ascertain the Pr protein’s chemical identity, distinguishing this protein from other acidic prealbumins that retain their typical electrophoretic pattern when treated with trypsin.
  • The research indicates that the Pr protein in horse serum closely corresponds to alpha-1-antitrypsin, based on the anti-tryptic effect revealed in the CPI-test and the purity test following its isolation.
  • This finding could have potentially significant implications in the field of equine health and veterinary medicine, providing insights into biochemical processes and disorders associated with this particular protein in horse serum.

Cite This Article

APA
Ek N. (1977). Identification of the PR prealbumin proteins in horse serum. Acta Vet Scand, 18(4), 458-470. https://doi.org/10.1186/BF03548409

Publication

Acta veterinaria Scandinavica
ISSN: 0044-605X
NlmUniqueID: 0370400
Country: England
Language: English
Volume: 18
Issue: 4
Pages: 458-470

Researcher Affiliations

Ek, N

    MeSH Terms

    • Animals
    • Chemical Precipitation
    • Electrophoresis, Starch Gel
    • Horses / blood
    • Phenotype
    • Prealbumin / analysis
    • Prealbumin / genetics
    • Serum Albumin / analysis
    • Trypsin
    • Trypsin Inhibitors / blood

    References

    This article includes 18 references
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    Citations

    This article has been cited 3 times.
    1. Keay G, Doxey DL. A study of the interaction between bromocresol green dye and bovine, ovine and equine serum globulins.. Vet Res Commun 1984 Feb;8(1):25-32.
      doi: 10.1007/BF02214691pubmed: 6202048google scholar: lookup
    2. Braend M. Genetic variation of the equine serum protease inhibitor system Pi (Pr) characterized by an enzyme binding staining technique after starch gel electrophoresis.. Acta Vet Scand 1982;23(4):592-602.
      doi: 10.1186/BF03546778pubmed: 6188351google scholar: lookup
    3. Ek N. The characterization of equine prealbumin (Pr) proteins by antigen-antibody crossed electrophoresis.. Acta Vet Scand 1979;20(2):180-90.
      doi: 10.1186/BF03546610pubmed: 484403google scholar: lookup
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