Fractionation of the Protein Components of Human Erythrocyte Membranes

Carbohydrate portion of membrane-located mouse H-2 alloantigens

“…About 4-6 % of [3H]fucose incorporated into crude membranes exists in the H-2 alloantigen from tumor cells, while a much smaller per cent of membrane [3H]galactose, [14C]mannose, [3H,14C]glucosamine exists in the alloantigen. The finding that the H-2 glycoprotein is a distinct entity which comprises only a small amount of the membrane material fits with recent studies which suggest that rather than being comprised of a single or a small number of protein subunits, animal cell membranes in reality consist of a rather large array of proteins and glycoproteins of widely different molecular weight Holland, 1968, 1970;Rosenberg and Guidotti, 1969;Lenard, 1970;Meezan et al, 1969).…”

Characterization and Analysis of Frog Photoreceptor Membranes

“…The outer segment suspensions appear to have relatively less ATPase activity than reported for some other preparations (18,19). Very little protein, if any, is removed by the gentle procedures which are known to extract 50% of the protein of erythrocyte membranes (14). The components which appear in the first aqueous extract might include metabolic enzymes, which Futterman et al (20) have characterized, and also mucopolysaccharides.…”

Role of sulfhydryl groups in erythrocyte membrane structure

“…Recent elegant studies by Steck et al (1970Steck et al ( , 1971 and Steck (1972) have shown that only one major peptide (band III) and one major glycoprotein (band Gl) appear to traverse the entire membrane; these are the only residues not extracted by pCMBS. The peptides released by pCMBS are those that can also be eluted by simple changes in ionic strength (Mitchell and Hanahan, 1966; Rosenberg and Guidotti, 1969;Fairbanks et al, 1971) or by dilute al-kali with /3-mercaptoethanol (Steck, 1972) and are probably superficially attached to the inner membrane surface (Steck, 1972).…”