Microheterogeneity of rat alpha-fetoprotein.
A purified and homogeneous preparation of rat alpha-fetoprotein (AFP) was separated into two components, AFPa and AFPb, by polyacrylamide gel electrophoresis. These two components had a definite difference in electrostatic net charge and gave only a single band on sodium dodecyl sulfate-electrophoresis. Neuraminidase-treated AFP gave clearly separable, slower moving four to six and finally two components depending on the time of incubation with neuraminidase. The time-dependent conversion of each AFPa and AFPb into slower migrating components upon neuraminidase treatment was confirmed by re-electrophoresis of separated and similarly treated AFPa and AFPb.
D000818:Animals; D005326:Fetal Proteins / Q000032:analysis*; D009439:Neuraminidase; D051381:Rats; D000509:alpha-Fetoproteins / Q000032:analysis* / Q000302:isolation & purification
D005326:Fetal Proteins; D000509:alpha-Fetoproteins; D009439:Neuraminidase