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Home / Equine Research Bank / Biochem J / Isolation and characterization of latherin, a surface-active...
The Biochemical journal1986; 235(3); 645-650; doi: 10.1042/bj2350645

Isolation and characterization of latherin, a surface-active protein from horse sweat.

Abstract: A protein, latherin, with unusual surface activity was isolated from horse sweat by gel filtration and ion-exchange chromatography. The protein has a Stokes radius, determined by gel filtration, of 2.47 nm, and in the ultracentrifuge sediments as a single species with S20,W 2.05 S, indicating an Mr of 24,400. On SDS/polyacrylamide-gel electrophoresis the molecule behaves as a single peptide chain of apparent Mr 20,000. Latherin contains a high proportion of hydrophobic amino acids (37.2%), and the leucine content (24.5%) is exceptionally high. The unusual composition of the protein may account for apparent anomalies in the Mr of latherin determined by empirical methods. Evidence indicating that latherin is responsible for much of the surface activity of horse sweat was obtained by a simple assay for surface tension and by contact-angle measurements. Latherin adsorbs very readily at hydrophobic surfaces, rendering them wettable. A possible role for latherin in thermoregulation is proposed.
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Publication Date: 1986-05-01 PubMed ID: 3753435PubMed Central: PMC1146737DOI: 10.1042/bj2350645Google 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.

This research article talks about identification and study of a protein called latherin from horse sweat, which shows unusual surface activity. The article proposes the potential role of this protein in horses’ thermoregulation.

Research Methodology

  • The researchers isolated latherin, a protein from horse sweat by utilizing gel filtration and ion-exchange chromatography.
  • The molecular weight of the protein, referred to as Mr, was calculated using gel filtration and the measured Stokes radius.
  • SDS/polyacrylamide-gel electrophoresis was performed to identify the molecular structure of the protein as a single peptide chain.
  • The authors analyzed the amino acid composition of latherin, revealing a high percentage of hydrophobic amino acids which likely lead to its surface activity.

Findings

  • Latherin was found to contain a large percentage of hydrophobic amino acids (37.2%) and the content of leucine (24.5%), a particular type of amino acid, was exceptionally high.
  • Anomalies in the molecular weight of latherin, determined by conventional methods, were attributed to its unusual amino acid composition.
  • Latherin demonstrated substantial surface activity as it quickly absorbed at hydrophobic surfaces, making them wettable. This characteristic was assessed through a simple assay for surface tension and contact-angle measurements.

Conclusions and Proposed Role

  • The research highlighted latherin as an important component of the surface activity in horse sweat.
  • A potential thermoregulatory role for latherin was suggested, possibly by allowing improved heat transfer through the sweating process. The protein’s ability to reduce surface tension might increase the spread and evaporation rate of sweat, thus enhancing the cooling effect.

Cite This Article

APA
Beeley JG, Eason R, Snow DH. (1986). Isolation and characterization of latherin, a surface-active protein from horse sweat. Biochem J, 235(3), 645-650. https://doi.org/10.1042/bj2350645

Publication

The Biochemical journal
ISSN: 0264-6021
NlmUniqueID: 2984726R
Country: England
Language: English
Volume: 235
Issue: 3
Pages: 645-650

Researcher Affiliations

Beeley, J G
    Eason, R
      Snow, D H

        MeSH Terms

        • Amino Acids / analysis
        • Animals
        • Chromatography, Gel
        • Electrophoresis, Polyacrylamide Gel
        • Fatty Acid-Binding Proteins
        • Horses / metabolism
        • Molecular Weight
        • Proteins / isolation & purification
        • Surface Tension
        • Surface-Active Agents / isolation & purification
        • Sweat / analysis

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        This article includes 9 references
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