Hostname: page-component-77c89778f8-fv566 Total loading time: 0 Render date: 2024-07-17T04:02:33.571Z Has data issue: false hasContentIssue false

Endopeptidases from Plasmodium knowlesi

Published online by Cambridge University Press:  06 April 2009

E. Hempelmann
Affiliation:
Division of Parasitology, National Institute for Medical Research, Mill Hill, London NW7 1AA
R. J. M. Wilson
Affiliation:
Division of Parasitology, National Institute for Medical Research, Mill Hill, London NW7 1AA

Summary

Extracts of rhesus monkey erythrocytes infected with Plasmodium knowlesi were fractionated by polyacrylamide gel electrophoresis (PAGE) and several zones of endopeptidase activity were demonstrated by an imprint-digest method. The enzymes were active only under acid conditions; activity was detected at pH 3·2 but not between pH 6·4 and 8·9 using haemoglobin, albumin or erythrocyte lysate as the substrate. Optimized PAGE conditions separated highly active parasite enzymes with Rf values of 73, 63 and 53 (± 7%), as well as a red cell endopeptidase, Rf44. Of two other minor bands of activity, one was associated with platelets.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1980

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

Aikawa, M. (1977). Variations in structure and function during the life cycle of malaria parasites. Bulletin of the World Health Organization 55, 139–56.Google Scholar
Barrett, A. J. (1970). Cathepsin D. Purification of isoenzymes from human and chicken liver. Biochemical Journal 117, 601–7.CrossRefGoogle ScholarPubMed
Carter, R. (1978). Studies on enzyme variation in the murine malaria parasites Plasmodium berghei, P. yoelii, P. vinckei and P. chabaudi by starch gel electrophoresis. Parasitology 76, 241–67.CrossRefGoogle ScholarPubMed
Chan, V. L. & Lee, P. Y. (1974). Host cell specific proteolytic enzymes in Plasmodium berghei-infected erythrocytes. Southeast Asian Journal of Tropical Medicine and Public Health 5, 447–9.Google ScholarPubMed
Clarke, J. T. (1964). Simplified ‘Disc’ (polyacrylamide gel) electrophoresis. Annals of the New York Academy of Sciences 121, 428–36.CrossRefGoogle ScholarPubMed
Cook, L., Grant, P. T. & Kermack, W. O. (1961). Proteolytic enzymes of the erythrocytic forms of rodent and simian species of malarial plasmodia. Experimental Parasitology 11, 372–9.CrossRefGoogle Scholar
Cook, R. T., Aikawa, M., Rock, R. C., Little, W. & Sprinz, H. (1969). The isolation and fractionation of Plasmodium knowlesi. Military Medicine 134, 866–83.CrossRefGoogle ScholarPubMed
Davis, B. J. (1964). Disc electrophoresis. Annals of the New York Academy of Sciences 121, 404–27.CrossRefGoogle ScholarPubMed
Levy, M. R. & Chou, S. C. (1973). Activity of some properties of an acid proteinase from normal and Plasmodium berghei infected red cells. Journal of Parasitology 59, 1064–79.CrossRefGoogle ScholarPubMed
Levy, M. R., Siddiqui, W. A. & Chou, S. C. (1974). Acid protease activity in Plasmodium falciparum and Plasmodium knowlesi and ghosts of their respective host cells. Nature, London 247, 546–9.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 193, 265–75.CrossRefGoogle ScholarPubMed
Mitchell, G. H., Butcher, G. A. & Cohen, S. (1975). Merozoite vaccination against Plasmodium knowlesi malaria. Immunology 29, 397407.Google ScholarPubMed
Morrison, D. B. & Jeskey, H. A. (1948). Alteration in some constituents of the monkey erythrocyte infected with Plasmodium knowlesi as related to pigment formation. Journal of the National Malaria Society 7, 259–64.Google ScholarPubMed
Reichelt, D., Jacobsohn, E. & Haschen, R. J. (1974). Purification and properties of Cathepsin D from human erythrocytes. Biochimica et Biophysica Acta 341, 1526.CrossRefGoogle ScholarPubMed
Roberts, R. C., Zais, D. P., Marx, J. J. & Kreuhaft, M. W. (1977). Comparative electrophoresis of the proteins and proteases in the thermophilic actinomycetes. Journal of Laboratory and Clinical Medicine 90, 1076–85.Google ScholarPubMed
Sapolsky, A. J. & Woessner, J. F. (1972). Multiple forms of Cathepsin D from bovine uterus. Journal of Biological Chemistry 247, 2069–76.CrossRefGoogle ScholarPubMed
Sherman, I. W. (1977). Amino acid metabolism and protein synthesis in malarial parasites. Bulletin of the World Health Organization 55, 265–76.Google ScholarPubMed