Purification of rat liver plasma membranes by wheat-germ-agglutinin affinity partitioning.
Rat liver plasma membranes were separated from other cellular membranes by affinity partitioning in an aqueous polymer two-phase system by using the lectin wheat-germ agglutinin covalently bound to dextran as the affinity ligand. In borate buffer the bulk of membranes partitioned in the poly(ethylene glycol)-rich top phase, whereas plasma membranes were pulled selectively into the dextran-rich bottom phase in the presence of ligand. The purity and yield of plasma membranes prepared by lectin affinity partitioning and by conventional sucrose-density-gradient centrifugation was similar, as judged from marker-enzyme activities. The affinity procedure, not dependent on lengthy centrifugations, is fast and gentle and will be advantageous when studying labile components.
Biochemistry, Chemical Centre, Lund, Sweden.
A
A
Persson
B
B
Johansson
H
H
Olsson
B
B
Jergil
D000818:Animals; D002021:Buffers; D002458:Cell Fractionation; D002462:Cell Membrane; D002478:Cells, Cultured; D003911:Dextrans; D008024:Ligands; D008099:Liver / Q000648:ultrastructure*; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains; D014909:Wheat Germ Agglutinins
D002021:Buffers; D003911:Dextrans; D008024:Ligands; D014909:Wheat Germ Agglutinins