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Biochemical pharmacology1970; 19(6); 2083-2090; doi: 10.1016/0006-2952(70)90306-0

Comparative action of various kininogenases on crude horse plasma substrates.

Abstract: The kininogenase activity of trypsin, plasmin, plasma kallikrein and heated Bothrops venom was compared, using fresh, heated and heat-acid-denatured horse plasma as source of kininogen. The venom kininogenase was found to have the highest activity on fresh horse plasma, followed by plasmin and trypsin which were equally active, and plasma kallikrein which was half as active as plasmin on these substrates. Plasmin and trypsin released more kinin from heat-treated than from fresh plasma whereas kallikrein released half as much as it liberates from fresh plasma. On heat-aciddenatured plasma equal activity was found for plasmin, trypsin and Bothrops kininogenase while the activity of plasma kallikrein was one tenth of that of plasmin or trpysin. None of the enzymes studied released additional kinin from any of the substrates after activation with trypsin or plasmin. After activation with plasma kallikrein, plasmin, trypsin and Bothrops kininogenase released additional kinin from the three substrates used. The results are discussed pointing out the possible importance of plasmin in the kinin system. Plasmin can replace trypsin in the determination of plasma kininogen by the method of Diniz et al.13
Publication Date: 1970-06-01 PubMed ID: 4254788DOI: 10.1016/0006-2952(70)90306-0Google Scholar: Lookup
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  • Journal Article

Summary

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This study focused on comparing the activity of various kininogenase enzymes, such as trypsin, plasmin, plasma kallikrein, and heated Bothrops venom, with respect to their substrates: fresh, heated, and heat-acid-denatured horse plasma, to understand their role in the kinin system, particularly emphasizing the significance of plasmin.

Overview of Study Findings

  • The study found that among the tested enzymes, Bothrops venom kininogenase exhibited the highest activity on fresh horse plasma. Meanwhile, plasmin and trypsin showed equal activity levels, with plasma kallikrein’s activity being half that of plasmin on the same substrates.
  • Plasmin and trypsin released more kinin (a peptide that leads to blood vessel dilation) from heat-treated plasma compared to fresh plasma. In contrast, kallikrein released only half the amount of kinin it usually liberates from fresh plasma.
  • When applied to heat-acid-denatured plasma, plasmin, trypsin, and Bothrops kininogenase came out with equal activity. However, the activity of plasma kallikrein was significantly reduced, being only one tenth of that of plasmin or trypsin.
  • Another notable observation was that none of the enzymes under study released additional kinin from any of the substrates upon activation with trypsin or plasmin. Post plasma kallikrein activation, plasmin, trypsin, and Bothrops kininogenase, all released more kinin from the tested substrates.

Significance of Results and Future Implications

  • The research’s findings clearly imply the potential prominence of plasmin in the kinin system, an enzyme system that regulates blood pressure.
  • The study concluded that plasmin could replace trypsin in the determination of plasma kininogen through the method suggested by Diniz et al.13, reflecting the role plasmin could play in diagnostic processes and possibly future therapeutic applications.
  • With a clearer understanding of these enzymatic activities, researchers could potentially exploit them in drug development, specifically in combatting conditions related to blood pressure and cardiovascular health.

Cite This Article

APA
Budnitskaya P, Gapanhuk E, Henriques OB. (1970). Comparative action of various kininogenases on crude horse plasma substrates. Biochem Pharmacol, 19(6), 2083-2090. https://doi.org/10.1016/0006-2952(70)90306-0

Publication

ISSN: 0006-2952
NlmUniqueID: 0101032
Country: England
Language: English
Volume: 19
Issue: 6
Pages: 2083-2090

Researcher Affiliations

Budnitskaya, P
    Gapanhuk, E
      Henriques, O B

        MeSH Terms

        • Animals
        • Biological Assay
        • Blood / drug effects
        • Bradykinin / metabolism
        • Bradykinin / pharmacology
        • Chemical Phenomena
        • Chemistry
        • Enzyme Activation
        • Fibrinolysin / pharmacology
        • Guinea Pigs
        • Horses
        • Hot Temperature
        • Ileum / drug effects
        • Kallikreins / pharmacology
        • Kinetics
        • Kinins / metabolism
        • Peptide Hydrolases / pharmacology
        • Protein Denaturation
        • Snakes
        • Trypsin / pharmacology
        • Venoms

        Citations

        This article has been cited 1 times.
        1. Deshwal A, Phan P, Datta J, Kannan R, Thallapuranam SK. A Meta-Analysis of the Protein Components in Rattlesnake Venom. Toxins (Basel) 2021 May 23;13(6).
          doi: 10.3390/toxins13060372pubmed: 34071038google scholar: lookup