Decrease of red cell membrane fluidity and -SH groups due to XXXX conditions is counteracted by @entity12837 .

@entity1 @entity8691 @entity3363 @entity3902 @entity10638 @entity12837 @entity969 @entity3955 @entity1365 @entity1602 @entity413
@entity1 red cell membranes (ghosts) were treated by 5 min of incubation with fasting or hypo- and @entity1602 concentrations of @entity413 . This simulation of nondiabetic or diabetic conditions revealed an influence on membrane fluidity and on protein -SH reactivity. Protein -SH groups, measured with Ellman's reagent, generally behave in the same way as membrane fluidity determined with @entity3955 . Maximal values were obtained with 5 mM @entity413 , whereas decrease was observed above 10 mM @entity413 . Addition of @entity12837 (4 nmol/mg protein) resulted in a significant increase in membrane fluidity and titratable -SH groups at @entity413 concentrations of 10 mM and above. @entity3902 diminished titrable-SH groups and did not restore membrane fluidity. @entity10638 was only effective in restoration of -SH groups. By contrast to @entity413 , other @entity3363 such as @entity413 , @entity8691 , or @entity969 revealed no comparable changes on membrane fluidity and titratable membrane -SH groups between concentrations of 5 and 10 mM. The @entity1602 effects of @entity413 were corroborated with isolated, reconstituted membrane proteins and erythrocyte @entity413 carrier, indicating that, in general, the observed divergent biochemical/biophysical changes of the red cell membrane are influenced by the @entity413 transport protein @entity1365 . The natural R-form and the S-form of @entity12837 were compared with racemic R-/S-forms for their efficiencies in alterations of red cell membrane fluidity. Decreased fluidities in presence of 10 mM @entity413 were found to be influenced in differentiated ways: the S-form was highly active in increasing fluidity at 4 nmol/mg and increasingly less active up to 20 nmol/mg protein. By contrast the R-form of @entity12837 was moderately efficient in increasing fluidity through a larger concentration range between 4 and 80 nmol/mg protein.
