Influence of N-terminal amino acids & conjugation position to carrier on specificities of antibodies elicited by malaria peptides.
Artigo
em Inglês
| IMSEAR
| ID: sea-20322
ABSTRACT
The specificity of murine antibodies raised against structurally related peptides derived from a malaria parasite membrane protein was studied. The peptides were conjugated to bovine serum albumin (BSA) with 6-maleimido caproic acyl N-hydroxysuccinimide ester before immunization. Conjugation to BSA through a C-terminal or an internal cysteine residue elicited antibodies with noticeably different specificities. An N-terminal tripeptide sequence arginine-asparagine-asparagine had a dominant influence on the immunogenicity of the peptides. Such factors need to be taken into consideration while designing peptide-based immunogens.
Texto completo:
DisponíveL
Índice:
IMSEAR (Sudeste Asiático)
Assunto principal:
Fragmentos de Peptídeos
/
Ensaio de Imunoadsorção Enzimática
/
Anticorpos Antiprotozoários
/
Dados de Sequência Molecular
/
Proteínas de Protozoários
/
Sequência de Aminoácidos
/
Animais
/
Malária
/
Camundongos
/
Camundongos Endogâmicos BALB C
Idioma:
Inglês
Ano de publicação:
1994
Tipo de documento:
Artigo
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