Human erythrocyte membrane proteins of zone 4.5 exist as families of related proteins.
An analysis of the polypeptide composition of zone 4.5 of human erythrocyte membranes has been done by immunoautoradiographic and two-dimensional peptide mapping techniques. Results of these studies demonstrated that the Coomassie blue profile was constant, with 14 well-resolved bands present. Zone 4.5 polypeptides existed as at least four families of two or more components with closely related polypeptide backbones. The families could be distinguished on the basis of their extraction characteristics, immunological cross-reactivity, and two-dimensional peptide maps. One family was related to protein 4.1, one family was related to band 3, and two families were independent and not similar to other larger membrane proteins. The data show that all of the visualized bands in zone 4.5 do not have the same protein composition and that several closely related forms of some polypeptides are present.
D001798:Blood Proteins / Q000032:analysis*; D002458:Cell Fractionation; D004591:Electrophoresis, Polyacrylamide Gel; D004910:Erythrocyte Membrane / Q000032:analysis* / Q000648:ultrastructure; D006801:Humans; D008565:Membrane Proteins / Q000097:blood*; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D010750:Phosphoproteins / Q000097:blood; D014357:Trypsin
D001798:Blood Proteins; D008565:Membrane Proteins; D010446:Peptide Fragments; D010750:Phosphoproteins; D014357:Trypsin