Comparative studies on the analysis of glycosylation heterogeneity of sialic acid-containing glycoproteins using capillary electrophoresis.
Comparative studies concerning glycoform analysis of sialoglycoproteins by capillary electrophoresis were performed using a few separation modes hitherto reported. Glycoprotein samples examined in the present study were successfully separated to their respective glycoforms using surface-modified capillaries commercially available for capillary gas chromatography in the running buffer near their isoelectric points. The analysis times were less than 50 min and reproducibilities in migration times were excellent (less than 2.0% RSD for both run-to-run and day-to-day analyses). We present a method for the glycoform analysis of alpha1-acid glycoprotein in sera by simple pre-treatment as an application. The present technique will become one of the general methods for the evaluation of glycosylation heterogeneity of commercially available glycoprotein drugs.
Kinoshita
M
M
Faculty of Pharmaceutical Sciences, Kinki University, Higashi-osaka, Japan.
Murakami
E
E
Oda
Y
Y
Funakubo
T
T
Kawakami
D
D
Kakehi
K
K
Kawasaki
N
N
Morimoto
K
K
Hayakawa
T
T
D019075:Electrophoresis, Capillary / Q000379:methods*; D006023:Glycoproteins / Q000737:chemistry* / Q000302:isolation & purification; D006031:Glycosylation; D007525:Isoelectric Focusing; D019158:N-Acetylneuraminic Acid / Q000032:analysis*
D006023:Glycoproteins; D019158:N-Acetylneuraminic Acid