Structural basis of electrophoretic variants of rat alpha-fetoprotein.
The molecular basis for electrophoretic variations of rat alpha-fetoprotein was studied. Stepwise deglycosylations of proteins and radiolabeling of the sugars indicated that the number of such chains per molecule is two and one for the slow and fast variants, respectively.
Ehara
A
A
Department of Biochemistry, Hokkaido University School of Medicine, Sapporo, Japan.
Nishi
S
S
D000581:Amidohydrolases / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001202:Ascitic Fluid / Q000737:chemistry; D002241:Carbohydrates / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D006031:Glycosylation; D008114:Liver Neoplasms, Experimental / Q000737:chemistry; D008969:Molecular Sequence Data; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; D051381:Rats; D000509:alpha-Fetoproteins / Q000032:analysis / Q000737:chemistry*
D002241:Carbohydrates; D000509:alpha-Fetoproteins; D000581:Amidohydrolases; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase