Comparative study on the distribution of ovalbumin glycoforms by capillaryelectrophoresis

Two commercial turkey egg ovalbumins (TEOs) with different quantities of ma nnose, were further purified by reversed-phase high-performance liquid chro matography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis for e ither of the purified glycoproteins showed one big wide band and one close small band. Capillary electrophoresis was used for the investigation of the separation of glycoforms of both glycoproteins. The best resolution of the glycoforms was obtained, reproducibly, with 100 mM berate, 1.8 mM 1,4-diam inobutane and pH 8.6 electrophoretic buffer. At least 13 glycoform peaks co uld be separated for either of the two glycoproteins. Their glycoform patte rns were highly similar except for the conspicuous decrease in quantity of four glycoforms in the ovalbumin containing less mannose, compared to that of the other with more mannose. Coinjection electrophoresis of the two glyc oproteins indicated that almost every glycoform peak of the former exactly overlapped with its corresponding glycoform peak of the latter. These resul ts clearly indicated that the two TEOs possessed the same glycoform pattern s but differed in quantity at least four glycoforms. It was found that the glycoform. patterns were remarkably different between TEO and chicken egg o valbumin. (C) 1999 Elsevier Science B.V. All rights reserved.