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. 1991 Jan 1;273(Pt 1):173–177. doi: 10.1042/bj2730173

Purification of rat liver plasma membranes by wheat-germ-agglutinin affinity partitioning.

A Persson 1, B Johansson 1, H Olsson 1, B Jergil 1
PMCID: PMC1149895  PMID: 1703408

Abstract

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.

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Selected References

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