Structural comparison of the 68 kDa laminin-binding protein and 5'-nucleotidase from chicken muscular sources: evidence against a gross structural similarity of both proteins.
Biochim Biophys Acta
; 994(3): 258-63, 1989 Feb 23.
Article
en En
| MEDLINE
| ID: mdl-2465783
ABSTRACT
The 68 kDa laminin-binding protein purified from chicken skeletal muscle and the ectoenzyme 5'-nucleotidase from chicken gizzard are both able to interact with laminin. They were both shown to possess a nearly identical amino acid composition. The 79 kDa glycosylated form of 5'-nucleotidase can be transformed into an enzymatically active form by treatment with endoglycosidase F (Endo F). Deglycosylated (Endo F-treated) 5'-nucleotidase exhibits an apparent molecular mass of 68 kDa. Using immunological and finger-printing techniques, both proteins were analysed to determine their structural relatedness. The results obtained indicate that both proteins are not identical but may posses a few common peptides of yet unknown sequence and length.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Receptores Inmunológicos
/
Músculos
/
Nucleotidasas
Límite:
Animals
Idioma:
En
Revista:
Biochim Biophys Acta
Año:
1989
Tipo del documento:
Article