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Home / Equine Research Bank / Am J Vet Res / Catalase activity in equine semen.
American journal of veterinary research2000; 61(9); 1026-1030; doi: 10.2460/ajvr.2000.61.1026

Catalase activity in equine semen.

Abstract: To characterize the activity of catalase in equine semen. Methods: 15 stallions of known and unknown reproductive history. Methods: Seminal plasma was collected from raw equine semen by centrifugation, and samples of seminal plasma were frozen prior to assay for catalase activity. Tissue samples (n = 3 stallions) from the bulbourethral gland, prostate gland, vesicular gland, and testis were homogenized, and cauda epididymal fluid was collected for determination of catalase activity. Catalase activity was determined as an enzyme kinetic assay by the disappearance of H2O2 as measured by ultraviolet spectrophotometry. Results: Catalase activity in equine seminal plasma was 989.3 +/- 1678 U/ml (mean +/- SEM), and the specific activity of catalase in equine seminal plasma was 98.7 +/- 29.2 U/mg of protein. Specific activity of catalase in tissue homogenates was significantly higher in the prostate gland (954 +/- 270 U/mg of protein) than in the ampulla (59 +/- 5 U/mg of protein), bulbourethral gland (54 +/- 11 U/mg of protein), vesicular gland (39 +/- 3 U/mg of protein), cauda epididymal fluid (11 +/- 3 U/mg protein), or testis (54 +/- 6 U/mg of protein). Conclusions: Equine seminal plasma contains a high activity of catalase that is derived primarily from prostatic secretions. Procedures such as semen cryopreservation that remove most seminal plasma from semen may reduce the ability to scavenge H2O2 and thereby increase the susceptibility of spermatozoa to oxidative stress.
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Publication Date: 2000-09-08 PubMed ID: 10976731DOI: 10.2460/ajvr.2000.61.1026Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

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 study primarily concerns with the measurement of catalase activity in the semen of stallions. The research found that the seminal plasma in equine semen contains a high activity of catalase, which majorly originates from the secretions of the prostate gland. This indicates the potential vulnerability of spermatozoa to oxidative stress when procedures like semen cryopreservation, which remove most seminal plasma, are used.

Research Methodology

  • The researchers gathered semen samples from 15 stallions with either known or unknown reproductive history for the experiment.
  • The seminal plasma was collected from the raw equine semen by subjecting it to centrifugation. These samples were then frozen before the assay for catalase activity was conducted.
  • They also collected tissue samples from the bulbourethral gland, prostate gland, vesicular gland, and testis for determination of catalase activity.
  • Furthermore, the researchers gathered cauda epididymal fluid from three stallions for the same purpose.
  • The catalase activity was determined through an enzyme kinetic assay, which involves measuring the disappearance of H2O2 through ultraviolet spectrophotometry.

Key Findings

  • The catalase activity in equine seminal plasma was found to be 989.3 +/- 1678 U/ml (mean +/- SEM), and the specific activity of catalase was 98.7 +/- 29.2 U/mg of protein.
  • Compared to other tissues, the prostate gland showed significantly higher specific catalase activity (954 +/- 270 U/mg of protein) than the ampulla, bulbourethral gland, vesicular gland, cauda epididymal fluid, or testis.

Study Conclusions

  • The researchers concluded that the seminal plasma in equine semen has a high catalase activity that is mainly derived from prostatic secretions. Catalase, an enzyme that breaks down hydrogen peroxide into water and oxygen, plays a key role in protecting cells from oxidative damage.
  • The study shows that procedures such as semen cryopreservation, which usually remove most of the seminal plasma, could potentially decrease the catalase activity and thus leave spermatozoa more susceptible to damage from oxidative stress.

Cite This Article

APA
Ball BA, Gravance CG, Medina V, Baumber J, Liu IK. (2000). Catalase activity in equine semen. Am J Vet Res, 61(9), 1026-1030. https://doi.org/10.2460/ajvr.2000.61.1026

Publication

American journal of veterinary research
ISSN: 0002-9645
NlmUniqueID: 0375011
Country: United States
Language: English
Volume: 61
Issue: 9
Pages: 1026-1030

Researcher Affiliations

Ball, B A
  • Department of Population Health and Reproduction, School of Veterinary Medicine, University of California, Davis 95616, USA.
Gravance, C G
    Medina, V
      Baumber, J
        Liu, I K

          MeSH Terms

          • Amitrole / pharmacology
          • Animals
          • Catalase / analysis
          • Enzyme Inhibitors / pharmacology
          • Horses / metabolism
          • Hydrogen Peroxide / metabolism
          • Male
          • Semen / enzymology
          • Sodium Azide / pharmacology
          • Spectrophotometry, Ultraviolet / veterinary
          • Spermatozoa / enzymology

          Citations

          This article has been cited 7 times.
          1. Catalán J, Yánez-Ortiz I, Tvarijonaviciute A, González-Aróstegui LG, Rubio CP, Barranco I, Yeste M, Miró J. Seminal Plasma Antioxidants Are Related to Sperm Cryotolerance in the Horse.. Antioxidants (Basel) 2022 Jun 28;11(7).
            doi: 10.3390/antiox11071279pubmed: 35883774google scholar: lookup
          2. Usuga A, Tejera I, Gómez J, Restrepo O, Rojano B, Restrepo G. Cryoprotective Effects of Ergothioneine and Isoespintanol on Canine Semen.. Animals (Basel) 2021 Sep 22;11(10).
            doi: 10.3390/ani11102757pubmed: 34679779google scholar: lookup
          3. Saadeldin IM, Khalil WA, Alharbi MG, Lee SH. The Current Trends in Using Nanoparticles, Liposomes, and Exosomes for Semen Cryopreservation.. Animals (Basel) 2020 Dec 3;10(12).
            doi: 10.3390/ani10122281pubmed: 33287256google scholar: lookup
          4. Peña FJ, O'Flaherty C, Ortiz Rodríguez JM, Martín Cano FE, Gaitskell-Phillips GL, Gil MC, Ortega Ferrusola C. Redox Regulation and Oxidative Stress: The Particular Case of the Stallion Spermatozoa.. Antioxidants (Basel) 2019 Nov 19;8(11).
            doi: 10.3390/antiox8110567pubmed: 31752408google scholar: lookup
          5. Papas M, Catalán J, Fernandez-Fuertes B, Arroyo L, Bassols A, Miró J, Yeste M. Specific Activity of Superoxide Dismutase in Stallion Seminal Plasma Is Related to Sperm Cryotolerance.. Antioxidants (Basel) 2019 Nov 9;8(11).
            doi: 10.3390/antiox8110539pubmed: 31717586google scholar: lookup
          6. Heidari Nasirabadi M, Shirazi A, Kadivar A, Shams-Esfandabadi N, Mohebbi A, Ahmadi E. Sericin Ameliorates the Capacitation State and Chromatin Integrity of Frozen-Thawed Stallion Spermatozoa by Reducing Oxidative Stress.. Avicenna J Med Biotechnol 2019 Jul-Sep;11(3):245-252.
            pubmed: 31379998
          7. Plaza Davila M, Martin Muñoz P, Tapia JA, Ortega Ferrusola C, Balao da Silva C C, Peña FJ. Inhibition of Mitochondrial Complex I Leads to Decreased Motility and Membrane Integrity Related to Increased Hydrogen Peroxide and Reduced ATP Production, while the Inhibition of Glycolysis Has Less Impact on Sperm Motility.. PLoS One 2015;10(9):e0138777.
            doi: 10.1371/journal.pone.0138777pubmed: 26407142google scholar: lookup
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