Electrophoretic analysis of polypeptides and glycopeptides of erythrocyte membrane sampled from rats simulating mild insulin dependent diabetes mellitus.

In order to understand the molecular mechanism of reduced life span of diabetic erythrocyte, polypeptides and glycopeptides were analyzed by disc gel preparative sodium dodecyl sulphate polyacrylamide gel electrophoresis. An additional glycopeptide (244.5 kDa) and two additional polypeptides (39.81 and 144.5 kDa) were observed on glycopeptide and polypeptide gel profiles of mild insulin dependent diabetes mellitus (mIDDM) sample as compared to control. On the basis of molecular weight, their position on gel profile and their widely accepted nomenclature they were termed as glycosylated-ankyrin, membrane accreted glyceraldehyde-3-phosphate dehydrogenease (G 3-PD) and stress induced band 2.3 peptide. Earlier we have reported an increase in heterogeneity associated with increase in the population of aged fragile cells having altered membrane bound cation dependent ATPases, cytosolic dehydrogenase and hexokinase activities of mIDDM simulating rat erythrocyte sample. Significance of above observation in view of our earlier observation is discussed to explain the molecular mechanism of reduced life span of diabetic erythrocytes.