Structural and biochemical analysis of the Mcleod erythrocyte membrane. I. Freeze fracture and discontinuous polyacrylamide gel electrophoresis analysis.
The abnormal erythrocyte of the McLeod phenotype displays a reduced Kell blood group expression, an abnormal morphology in about 30% of the total red blood cell population and a decrease in water permeability. These parameters have previously been shown to be independent of membrane lipid composition, microviscosity and electrolyte transport. Findings such as these seem to implicate the involvement of a defective membrane protein. The present study investigated membrane composition by utilizing two techniques: freeze-fracture electron microscopy and discontinuous polyacrylamide gel electrophoresis. Electrophoretic scans revealed no apparent band additions or deletions showing McLeod membrane protein composition to be normal. Freeze-fracture electron microscopy did show a significant increase in intramembrane particle density. These findings may be resolved by proposing a dissociation of the band 3 glycoprotein. Unlinkage of this polypeptide, thought to be involved in water transport and intramembranous particle composition, could account for the decreased water transport and increased particle density seen in the McLeod erythrocyte membrane.
D001789:Blood Group Antigens; D002463:Cell Membrane Permeability; D004591:Electrophoresis, Polyacrylamide Gel; D004910:Erythrocyte Membrane / Q000276:immunology / Q000648:ultrastructure; D004912:Erythrocytes; D004913:Erythrocytes, Abnormal; D005614:Freeze Fracturing; D006801:Humans; D007626:Kell Blood-Group System; D008297:Male; D008565:Membrane Proteins; D010316:Particle Size
D001789:Blood Group Antigens; D007626:Kell Blood-Group System; D008565:Membrane Proteins