Glycoform analysis of alpha₁-acid glycoprotein by capillary electrophoresis.

ABSTRACT: A relatively fast and reproducible CE separation was developed for the glycoform analysis of α₁-acid glycoprotein (AGP). Factors that were considered included the pH for this separation and various techniques for coating the capillary and/or to minimize electroosmotic flow and protein adsorption. Optimum resolution of the AGP glycoforms was obtained at pH 4.2 with a running buffer containing 0.1% Brij 35 and by using static and dynamic coatings of PEO on the capillary. These conditions made it possible to separate nine AGP glycoform bands in about 20min. The limit of detection (based on absorbance measurements) ranged from 0.09 to 0.38μM for these AGP glycoform bands, and the linear range extended up to a total AGP concentration of at least 240μM. The migration times for the gly

SUBMITTER: Zhang C 

PROVIDER: S-EPMC5147584 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature