Influence of N-terminal amino acidsconjugation position to carrier on specificities of antibodies elicited by malaria peptides

Autor:	R, Ramasamy, C, Wickremaratne
Rok vydání:	1994
Předmět:	Mice Mice Inbred BALB C Antibody Specificity Molecular Sequence Data Protozoan Proteins Animals Antibodies Protozoan Enzyme-Linked Immunosorbent Assay Amino Acid Sequence Peptide Fragments Malaria
Zdroj:	The Indian journal of medical research. 99
ISSN:	0971-5916
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::e72546365dc584ace42ebba5bf22b512 https://pubmed.ncbi.nlm.nih.gov/8163297 Zobrazit plný text záznamu