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Human transcobalamin isopeptides: Separation by isoelectric focusing and by polyacrylamide gel electrophoresis
Author(s) -
Hansen Mads,
FràterSchröder Marijke
Publication year - 1987
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150080503
Subject(s) - isoelectric focusing , polyacrylamide gel electrophoresis , isoelectric point , chromatography , polyacrylamide , electrophoresis , chemistry , gel electrophoresis of proteins , gel electrophoresis , biochemistry , enzyme , polymer chemistry
Transcobalamin was separated by isoelectric focusing and by polyacrylamide gel electrophoresis. Isoelectric focusing showed one band in homozygotes and two bands in heterozygotes, with isoelectric points between 6.3 and 7.0, while polyacrylamide gel electrophoresis produced two and four bands, respectively. Addition of neuraminidase, urea or EDTA had no effect on the separation of transcobalamin at isoelectric focusing. The results obtained by the two methods are comparable and in accord with the nomenclature of transcobalamin variants.