Structure verification of a recombinant chimeric anti-CD20 IgG1 monoclonal antibody / 药学学报
Acta Pharmaceutica Sinica
; (12): 752-755, 2010.
Article
en Zh
| WPRIM
| ID: wpr-354538
Biblioteca responsable:
WPRO
ABSTRACT
Structure of a recombinant chimeric anti-CD20 IgG1 monoclonal antibody was verified by the application of high-performance liquid chromatography-mass spectrometry (HPLC-MS)and N-terminal sequencer. Molecular masses, N-terminal sequences and peptide maps of the antibody treated with different reagents and enzymes were measured. Results indicate that the amino acid sequences of light and heavy chains and 10 disulfide bonds were consistent with theoretical structure. By comparison of molecular masses and peptide maps for the fully glycosylated and deglycosylated samples, the N-linked glycosylation site was identified. The method is simple, rapid, precise, and could be referred to the quality control and structure determination of other IgG1 products.
Texto completo:
1
Base de datos:
WPRIM
Asunto principal:
Espectrometría de Masas
/
Glicosilación
/
Mapeo Peptídico
/
Proteínas Recombinantes
/
Inmunoglobulina G
/
Tripsina
/
Química
/
Cromatografía Líquida de Alta Presión
/
Secuencia de Aminoácidos
/
Cadenas Pesadas de Inmunoglobulina
Tipo de estudio:
Prognostic_studies
Idioma:
Zh
Revista:
Acta Pharmaceutica Sinica
Año:
2010
Tipo del documento:
Article