caa a22 4500 469115475 CHVBK 20180323133123.0 cr unu---uuuuu 170328e19920401xx s 000 0 eng 10.1007/BF00731704 doi (NATIONALLICENCE)springer-10.1007/BF00731704 Separation and analysis of the glycoform populations of ribonuclease B using capillary electrophoresis [Elektronische Daten] [Pauline Rudd, Ian Scragg, Eva Coghill, Raymond Dwek] The development of methods to separate, analyse and monitor changes in glycoform populations is essential if a more detailed understanding of the structure, function and processing of glycoproteins is to emerge. In this study, intact ribonuclease B was resolved by borate capillary electrophoresis into five populations according to the particular oligomnnose structure associated with each glycoform. The relative proportions of these populations are correlated with the percentages obtained indirectly by analysis of the hydrazine released oligosaccharides using Bio-Gel P-4 gel filtration, matrix assisted laser desorption mass spectrometry and high performance anion exchange chromatography. Alterations in the composition of the glycoform populations during digestion of ribonuclease B withA. saitoi α(1-2)mannosidase were monitored by capillary electrophoresis (CE). Digestion of the free oligosaccharides under the same conditions, monitored by anion exchange chromatography, revealed a difference in rate, allowing some insight into the role of the protein during oligosaccharide processing. In conjunction with other methods, this novel application of CE may prove a useful addition to the techniques available for the study of glycoform populations. Chapman & Hall, 1992 Capillary electrophoresis nationallicence glycoforms nationallicence oligomannose nationallicence ribonuclease B nationallicence Rudd Pauline Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, OX1 3QU, Oxford, UK aut Scragg Ian Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, OX1 3QU, Oxford, UK aut Coghill Eva Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, OX1 3QU, Oxford, UK aut Dwek Raymond Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, OX1 3QU, Oxford, UK aut Glycoconjugate Journal Kluwer Academic Publishers 9/2(1992-04-01), 86-91 0282-0080 9:2<86 1992 9 10719 https://doi.org/10.1007/BF00731704 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00731704 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Rudd Pauline Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, OX1 3QU, Oxford, UK aut NATIONALLICENCE 700 1- Scragg Ian Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, OX1 3QU, Oxford, UK aut NATIONALLICENCE 700 1- Coghill Eva Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, OX1 3QU, Oxford, UK aut NATIONALLICENCE 700 1- Dwek Raymond Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, OX1 3QU, Oxford, UK aut NATIONALLICENCE 773 0- Glycoconjugate Journal Kluwer Academic Publishers 9/2(1992-04-01), 86-91 0282-0080 9:2<86 1992 9 10719 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer