An abnormal human IgA1 half-molecule.
Biochim Biophys Acta
; 494(2): 326-31, 1977 Oct 26.
Article
em En
| MEDLINE
| ID: mdl-410452
ABSTRACT
An IgA1 half-molecule, which is composed of a deleted alpha1 chain linked with a disulfide bond to an intact kappa chain, was detected in a patient (Cha). The molecular weights of the paraprotein and the isolated alpha1 chain were estimated to be 75 000 and 53 000, respectively. Identification of tyrosine as the C-terminal amino acid and the presence of idiotypic determinants in the abnormal alpha1 chain indicated that the molecule would have an intact N-terminal variable region and a C-terminal region. Furthermore, no cleavage of the abnormal protein into Fab and Fc by proteolytic enzyme isolated from Neisseria gonorrhoeae suggested the absence of a "hinge" region in the abnormal alpha1 chain.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Imunoglobulina A
/
Cadeias alfa de Imunoglobulina
/
Cadeias Pesadas de Imunoglobulinas
Tipo de estudo:
Prognostic_studies
Limite:
Humans
Idioma:
En
Ano de publicação:
1977
Tipo de documento:
Article