Literature DB >> 6768047

Endopeptidases from Plasmodium knowlesi.

E Hempelmann, R J Wilson.   

Abstract

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.

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Year:  1980        PMID: 6768047     DOI: 10.1017/s0031182000000780

Source DB:  PubMed          Journal:  Parasitology        ISSN: 0031-1820            Impact factor:   3.234


  4 in total

Review 1.  Malaria parasite plasmepsins: More than just plain old degradative pepsins.

Authors:  Armiyaw S Nasamu; Alexander J Polino; Eva S Istvan; Daniel E Goldberg
Journal:  J Biol Chem       Date:  2020-05-04       Impact factor: 5.157

Review 2.  Comparative biochemistry of the proteinases of eucaryotic microorganisms.

Authors:  M J North
Journal:  Microbiol Rev       Date:  1982-09

3.  Hemoglobin degradation in the malaria parasite Plasmodium falciparum: an ordered process in a unique organelle.

Authors:  D E Goldberg; A F Slater; A Cerami; G B Henderson
Journal:  Proc Natl Acad Sci U S A       Date:  1990-04       Impact factor: 11.205

4.  Hemoglobin degradation in the human malaria pathogen Plasmodium falciparum: a catabolic pathway initiated by a specific aspartic protease.

Authors:  D E Goldberg; A F Slater; R Beavis; B Chait; A Cerami; G B Henderson
Journal:  J Exp Med       Date:  1991-04-01       Impact factor: 14.307

  4 in total

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