Purification and characterization of IgG1 and IgG2 from buffalo (Bubalus bubalis) serum and colostrum.
Vet Immunol Immunopathol
; 37(1): 61-71, 1993 Jun.
Article
em En
| MEDLINE
| ID: mdl-8342260
ABSTRACT
Buffalo IgG1 and IgG2 were purified from serum and colostrum using salt precipitation, dialysis, gel filtration and ion-exchange chromatography. Their purity was monitored by immunodiffusion and immunoelectrophoresis using anti-heavy chain specific sera and SDS-PAGE. Selective binding of IgG2 to protein-A was used to remove IgG2 from IgG1 preparations. The IgG1 and IgG2 had a molecular mass (Mr) of 162.0 and 161.5 kD, respectively and were found to consist of heavy (H) and light (L) chains. The H and L chains had Mr of 58 and 24 kD, respectively. Reduction-alkylation followed by gel filtration was used for the isolation of H and L chains. While intact H chains were obtained, the L chains appeared to be cleaved into 14 kD molecules and smaller fragments. The mean hexoses content of the serum IgG1 and IgG2 was 1.81 +/- 0.02% and 0.70 +/- 0.02%, respectively. The corresponding values for colostral IgG1 and IgG2 were 1.76 +/- 0.01% and 0.78 +/- 0.08%. Both the IgG subclasses activated homologous complement. These results suggest that buffalo and cattle IgG subclasses have many common characteristics and minor differences.
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Base de dados:
MEDLINE
Assunto principal:
Imunoglobulina G
/
Búfalos
/
Colostro
Idioma:
En
Revista:
Vet Immunol Immunopathol
Ano de publicação:
1993
Tipo de documento:
Article
País de afiliação:
Índia