Hostname: page-component-848d4c4894-4rdrl Total loading time: 0 Render date: 2024-07-05T01:13:10.949Z Has data issue: false hasContentIssue false
  • English
  • Français

An analysis of the proteinases of Trichomonas vaginalis by polyacrylamide gel electrophoresis

Published online by Cambridge University Press:  06 April 2009

G. H. Coombs  and
M. J. North
G. H. Coombs
Affiliation:
Department of Zoology, University of Glasgow, Glasgow G12 8QQ and Department of Biological Science, University of Stirling, Stirling FK9 4LA
M. J. North
Affiliation:
Department of Zoology, University of Glasgow, Glasgow G12 8QQ and Department of Biological Science, University of Stirling, Stirling FK9 4LA
Get access Rights & Permissions [Opens in a new window]

Summary

The proteinases of Trichomonas vaginalis have been analysed by electrophoresis in polyacrylamide gels containing denatured haemoglobin. Seven bands of activity were detected indicating multiple proteinases. All of the enzymes were stimulated by 1 mM dithiothreitol and had inhibitor sensitivities characteristic of cysteine proteinases. The enzymes differed significantly, however, with respect to pH optima and relative sensitivities to inhibitors.

Type
Research Article
Information
Parasitology , Volume 86 , Issue 1 , February 1983 , pp. 1 - 6
Copyright
Copyright © Cambridge University Press 1983

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Barrett, A. J. & McDonald, J. K. (1980). Mammalian Proteinases: A Glossary and Bibliography, vol. 1, Endopeptidases. London and New York: Academic Press.Google Scholar
Coombs, G. H. (1976). Studies on the activity of nitroimidazoles. In Biochemistry of Parasites and Host–Parasite Relationships (ed. Van den Bossche, H.), pp. 545–52. Amsterdam: Elsevier/North Holland Biomedical Press.Google Scholar
Coombs, G. H. (1982). Proteinases of Leishmania mexicana and other flagellate protozoa. Parasitology 84, 149–55.CrossRefGoogle ScholarPubMed
Coombs, G. H., Hart, D. T. & Capaldo, J. (1982). Proteinase inhibitors as antileishmanial agents. Transactions of the Royal Society of Tropical Medicine and Hygiene (in the Press).CrossRefGoogle Scholar
Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. (1951). Protein measurement with the folin phenol reagent. Journal of Biological Chemistry 196, 265–75.CrossRefGoogle Scholar
McLaughlin, J. & Muller, M. (1979). Purification and characterization of a low molecular weight thiol proteinase from the flagellate, protozoon Tritrichomonas foetus. Journal of Biological Chemistry 254, 1526–33.CrossRefGoogle ScholarPubMed
Muller, M. (1973). Biochemical cytology of trichomonad flagellates. I. Subcellular localization of hydrolases, dehydrogenases, and catalase in Tritrichomonas foetus. Journal of Cell Biology 57, 453–74.Google ScholarPubMed
North, M. J. (1982). Comparative biochemistry of the proteinases of eucaryote microorganisms. Microbiological Reviews (in the press).CrossRefGoogle Scholar
North, M. J. & Coombs, G. H. (1981). Proteinases of Leishmania mexicana amastigotes and promastigotes: analysis by gel electrophoresis. Molecular and Biochemical Parasitology 3, 293–300.CrossRefGoogle ScholarPubMed