Spectrin oligomers of the red cell membrane extracts in hereditary spherocytosis.

Spectrin oligomers were extracted from the erythrocyte membrane at 37 degrees C with the low ionic strength buffer. The spectrin extractability of HS membranes was enhanced compared with controls in some cases. The major spectrin component in the extract was dimer which was, apart from a tetramer, purified by gel filtration on the Sepharose 4B column. No changes of dimer-tetramer interconversion in the extract from HS membranes were observed. Similarly, the protein composition of the membrane extracts from two types of red cells remained unchanged.