Literature DB >> 3323905

Purification of a Plasmodium berghei neutral endopeptidase and its localization in merozoite.

F Bernard1, J Schrével.   

Abstract

A Plasmodium berghei neutral endopeptidase specific for the fluorogenic substrates valyl-leucyl-glycyl-arginyl/lysyl-aminoethyl-carbazole was purified by Fast Protein Liquid Chromatography. The enzyme was a Mr 68,000 polypeptide. Immunization of mice with the purified enzyme gave a specific antiserum, as demonstrated by immunoblotting. Immunofluorescence with this antiserum showed a strong labelling of P. berghei merozoites in mature segmented schizonts and of merozoites released from schizont-infected red blood cell. This labelling was mainly associated with the merozoite apex. It is possible that this endopeptidase is involved in the reinvasion.

Entities:  

Mesh:

Substances:

Year:  1987        PMID: 3323905     DOI: 10.1016/0166-6851(87)90140-x

Source DB:  PubMed          Journal:  Mol Biochem Parasitol        ISSN: 0166-6851            Impact factor:   1.759


  4 in total

1.  Looking for the exit: How do malaria parasites escape from red blood cells?

Authors:  L H Bannister
Journal:  Proc Natl Acad Sci U S A       Date:  2001-01-16       Impact factor: 11.205

2.  Rapid transport of the acidic phosphoproteins of Plasmodium berghei and P. chabaudi from the intraerythrocytic parasite to the host membrane using a miniaturized fractionation procedure.

Authors:  M F Wiser; H N Lanners
Journal:  Parasitol Res       Date:  1992       Impact factor: 2.289

3.  Purification and identification of a neutral endopeptidase in Plasmodium falciparum schizonts and merozoites.

Authors:  P Grellier; I Picard; F Bernard; R Mayer; H G Heidrich; M Monsigny; J Schrével
Journal:  Parasitol Res       Date:  1989       Impact factor: 2.289

Review 4.  Proteases of malaria parasites: new targets for chemotherapy.

Authors:  P J Rosenthal
Journal:  Emerg Infect Dis       Date:  1998 Jan-Mar       Impact factor: 6.883

  4 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.