[Electrophoretic variants of rat alpha-fetoprotein].
It has been well documented that rat AFP is separated into two discrete fractions electrophoretically and by ion exchange chromatography and it is generally accepted that the two forms of AFP, "Slow" and "Fast" variants, have different charges and molecular sizes. In this paper, the molecular basis of electrophoretic variants of rat alpha-fetoprotein (AFP) was studied. Carbohydrate-free rat AFP was electrophoretically homogeneous. Stepwise conversion of molecular sizes by deglycosylation with glycopeptidase F and the specific activities of the variants of which sugar chains were radiolabelled suggest that "Slow" and "Fast" variants have two and one sugar chains per molecule, respectively.
Ehara
A
A
Department of Biochemistry, Hokkaido University School of Medicine, Sapporo, Japan.
D000581:Amidohydrolases; D000818:Animals; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D007526:Isoelectric Point; D008970:Molecular Weight; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; D051381:Rats; D011919:Rats, Inbred Strains; D014415:Tunicamycin; D000509:alpha-Fetoproteins / Q000737:chemistry / Q000302:isolation & purification*
D000509:alpha-Fetoproteins; D014415:Tunicamycin; D000581:Amidohydrolases; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase