The sites of tryptic cleavage in bovine secretory component: structural and functional implications.
Biochim Biophys Acta
; 912(3): 365-70, 1987 Apr 30.
Article
en En
| MEDLINE
| ID: mdl-3567207
ABSTRACT
Tryptic fragments from bovine secretory component and sIgA have been separated by HPLC and/or SDS polyacrylamide gel electrophoresis and electroblotting. Their N-terminal amino acid sequences have been determined and their positions in the secretory component molecule deduced by homology with the amino acid sequences of human secretory component and rabbit polyimmunoglobulin receptor. Taken in conjunction with the known binding affinities of the tryptic fragments, the results imply that the three most N-terminal domains of secretory component are directly involved in binding IgM and IgA dimers. The results also favour the concept of an extended 'zig-zag' structure for the secretory component molecule.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Fragmentos de Péptidos
/
Componente Secretorio
/
Fragmentos de Inmunoglobulinas
/
Tripsina
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Biochim Biophys Acta
Año:
1987
Tipo del documento:
Article