TY - JOUR
T1 - Fine structure of the band 3 protein in human red cell membranes
T2 - Freeze-fracture studies
AU - Weinstein, R. S.
AU - Khodadad, J. K.
AU - Steck, T. L.
PY - 1978
Y1 - 1978
N2 - The major red cell membrane protein, band 3, is a glycoprotein which extends across the membrane from the extracellular space into the cytoplasmic compartment. It is widely held that band 3 is a component of the intramembrane particles (IMP) which can be demonstrated by freeze-fracture electron microscopy. The outer surface poles of the IMP can be seen by freeze-etching after they are unmasked by proteolysis under conditions which excise the surrounding sialopeptides from the membrane. The poles appear as distinctive projections, 30-50 Ȧ in diameter, the 'ES particles'. The ES particles remain associated with the outer surface of the membrane following cleavage of the band 3 polypeptide by chymotrypsin or pronase. This is consistent with previous biochemical studies which have shown that the 38,000-dalton outer surface segment of band 3 is intercalated in the lipid bilayer. A granulofibrillar component at the inner surface of the membrane is provisionally identified as the 40,000-dalton inner-surface domain of band 3.
AB - The major red cell membrane protein, band 3, is a glycoprotein which extends across the membrane from the extracellular space into the cytoplasmic compartment. It is widely held that band 3 is a component of the intramembrane particles (IMP) which can be demonstrated by freeze-fracture electron microscopy. The outer surface poles of the IMP can be seen by freeze-etching after they are unmasked by proteolysis under conditions which excise the surrounding sialopeptides from the membrane. The poles appear as distinctive projections, 30-50 Ȧ in diameter, the 'ES particles'. The ES particles remain associated with the outer surface of the membrane following cleavage of the band 3 polypeptide by chymotrypsin or pronase. This is consistent with previous biochemical studies which have shown that the 38,000-dalton outer surface segment of band 3 is intercalated in the lipid bilayer. A granulofibrillar component at the inner surface of the membrane is provisionally identified as the 40,000-dalton inner-surface domain of band 3.
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U2 - 10.1002/jss.400080310
DO - 10.1002/jss.400080310
M3 - Article
C2 - 723268
AN - SCOPUS:0018168653
SN - 0730-2312
VL - 8
SP - 325
EP - 335
JO - Journal of Supramolecular and Cellular Biochemistry
JF - Journal of Supramolecular and Cellular Biochemistry
IS - 3
ER -