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Freeze–thaw immobilization of liposomes in chromatographic gel beads: evaluation by confocal microscopy and effects of freezing rate
Author(s) -
Lundqvist Andreas,
Ocklind Göran,
Haneskog Lars,
Lundahl Per
Publication year - 1998
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/(sici)1099-1352(199812)11:1/6<52::aid-jmr389>3.0.co;2-k
Subject(s) - liposome , agarose , chromatography , confocal laser scanning microscopy , membrane , confocal , chemistry , confocal microscopy , chemical engineering , biophysics , biochemistry , geometry , mathematics , microbiology and biotechnology , biology , engineering
Biological membranes immobilized in chromatographic gel beads constitute a multifunctional affinity matrix. Membrane protein–solute interactions and drug partitioning into the lipid bilayers can conveniently be studied. By the use of confocal laser‐scanning microscopy (CLSM) the distribution of immobilized model membranes in the beads has been visualized for the first time. Freeze–thaw‐immobilized liposomes in Superdex 200 gel beads were situated in a thick shell surrounding a liposome‐free core. The amount of phospholipids immobilized by freeze–thawing was dependent on the temperature in the cooling bath and the type of test tube used. A bath temperature of −25 °C gave higher immobilization yield than freezing at −75 or −8 °C did. Freeze–thawing in the presence of liposomes did not affect the gel bead shape or the refractive index homogeneity of the agarose network of the beads, as shown by confocal microscopy. Copyright © 1998 John Wiley & Sons, Ltd.