Artigo Revisado por pares

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

1987; Elsevier BV; Volume: 26; Issue: 1-2 Linguagem: Inglês

10.1016/0166-6851(87)90140-x

ISSN

1872-9428

Autores

François Bernard, Joseph Schrével,

Tópico(s)

Venomous Animal Envenomation and Studies

Resumo

A Plasmodium berghei neutral endopeptidase specific for the fluorogenic substrates valyl-leucyl-glycyl-arginyl/lysyl-aminoethylcarbazole 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.

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