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Biological chemistry Hoppe-Seyler1985; 366(8); 705-712; doi: 10.1515/bchm3.1985.366.2.705

Proteinase inhibitors of horse seminal plasma. A high molecular mass, acid-soluble proteinase inhibitor.

Abstract: Horse seminal plasma does not possess a proteinase inhibitor corresponding to human HUSI-I (human seminal plasma inhibitor). Instead a protein complex of high relative molecular mass (Mr) containing proteinase inhibitory activity was detected, which was called horse seminal plasma protein complex or HSPC. The compound had a broad enzyme-inhibiting spectrum. Its Mr was estimated to be 800 000 and it was composed of 7 different polypeptides with Mr values ranging from 11 000 to 30 000. Its carbohydrate content was between 3.5% and 5%. Despite the high molecular mass, the complex was soluble in diluted perchloric acid and did not lose its biological activity. The high recovery of seminal plasma protein (69%) after perchloric acid treatment, the unaltered immunoelectrophoretic precipitation pattern of the perchloric acid soluble part of seminal plasma, and the similarity of the polypeptide patterns of unfractionated seminal plasma and HSPC suggest that HSPC is one of the major components of horse seminal plasma. In addition to HSPC, horse seminal plasma contained a group of three electrophoretically distinguishable proteinase inhibitors, corresponding roughly to a Mr of 6500. They inhibited only trypsin. The similar Mr values and the identical narrow enzyme specificity suggest that they are isoinhibitors and may be analogues of human HUSI-II (human seminal plasma inhibitor). The lack of a HUSI-I analog in the horse is discussed in relation to a previously made observation that horse tracheobronchial fluid contains no detectable perchloric acid-soluble proteinase inhibitors.
Publication Date: 1985-08-01 PubMed ID: 2998413DOI: 10.1515/bchm3.1985.366.2.705Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

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This research article focuses on the identification and analysis of a protein complex in horse seminal plasma that acts as a proteinase inhibitor. Interestingly, this complex does not correspond to the equivalent inhibitor identified in human seminal plasma.

Key Findings

  • The research identifies the presence of a high relative molecular mass proteinase inhibitor within horse seminal plasma. Unlike in humans, the horse seminal plasma does not contain a proteinase inhibitor equivalent to human HUSI-I.
  • Named the Horse Seminal Plasma Protein Complex (HSPC), this component has a broad range of enzyme-inhibiting abilities. Its relative molecular mass is approximately 800,000.
  • The HSPC is composed of seven different polypeptides with relative molecular mass values that range between 11,000 and 30,000. Further, it is found to contain between 3.5% and 5% carbohydrate content.
  • Despite its high molecular mass, the HSPC is soluble even in dilute perchloric acid, and its inhibitory activities remain unaffected. The substantial recovery (69%) of seminal plasma protein after perchloric acid treatment suggests that HSPC is a significant component of horse seminal plasma.

Additional Observations

  • Apart from the HSPC, the horse seminal plasma was found to contain another group of three distinct proteinase inhibitors. These demonstrated a relative molecular mass roughly around 6,500 and were only able to inhibit trypsin.
  • The similar molecular mass and identical enzyme specificity of these inhibitors suggest that they might be isoinhibitors and could potentially be analogous to human HUSI-II.
  • The absence of a human HUSI-I equivalent in horse seminal plasma is discussed in the research. This observation is compared with a previous finding that horse tracheobronchial fluid contains no identifiable proteinase inhibitors soluble in perchloric acid.

Cite This Article

APA
von Fellenberg R, Zweifel HR, Grünig G, Pellegrini A. (1985). Proteinase inhibitors of horse seminal plasma. A high molecular mass, acid-soluble proteinase inhibitor. Biol Chem Hoppe Seyler, 366(8), 705-712. https://doi.org/10.1515/bchm3.1985.366.2.705

Publication

ISSN: 0177-3593
NlmUniqueID: 8503054
Country: Germany
Language: English
Volume: 366
Issue: 8
Pages: 705-712

Researcher Affiliations

von Fellenberg, R
    Zweifel, H R
      Grünig, G
        Pellegrini, A

          MeSH Terms

          • Animals
          • Chromatography, Agarose
          • Chromatography, Gel
          • Electrophoresis, Agar Gel
          • Horses / metabolism
          • Male
          • Molecular Weight
          • Perchlorates / pharmacology
          • Protease Inhibitors / isolation & purification
          • Semen / analysis

          Citations

          This article has been cited 1 times.
          1. Lung O, Tram U, Finnerty CM, Eipper-Mains MA, Kalb JM, Wolfner MF. The Drosophila melanogaster seminal fluid protein Acp62F is a protease inhibitor that is toxic upon ectopic expression. Genetics 2002 Jan;160(1):211-24.
            doi: 10.1093/genetics/160.1.211pubmed: 11805057google scholar: lookup