[Erythrocyte membrane proteins during exposure to moderately low temperatures].

The electrophoretic analysis of erythrocyte membrane proteins after cooling the reconstituted cells to moderately low temperatures (-30 degrees divided by -70 degrees C) has demonstrated that freezing at slow rates results in an increase in the oligomerization capability of spectrine, the main membrane skeleton protein and band 3 protein under the effect of diamide--a thioloxidizing agent. The data obtained testify to the fact that the membrane is a relatively cryoresistant cellular component at more rapid cooling rates in the presence of cryoprotective compounds.

[Effect of moderately low temperatures (-30 C to -70 C) on the permeability of erythrocyte membranes].

The barrier properties of reconstituted and native erythrocyte membranes frozen to -30, -40 or -70 degrees C and stored for a month were studied. The release of markers, namely haemoglobin molecules, [14C] sucrose and K+ ions from cells and membrane structures was measured. The main changes in the barrier function of ghosts and cells have been found to be due to freeze-thawing rather than to storage conditions.