Human erythrocyte band 3 (EPB3) polymorphism: Analysis of blood and bloodstains by an immunodetection method and frequency of the EPB3* Memphis variant

1993 ◽  
Vol 106 (1) ◽  
pp. 1-4
Author(s):  
Akihiko Kimura ◽  
Tomoji Uda ◽  
Shoichi Nakashima ◽  
Haruhiko Ikeda ◽  
Seiji Yasuda ◽  
...  
Keyword(s):  
Human Erythrocyte ◽  
Band 3 ◽  
Polymorphism Analysis

scholarly journals Ultrastructure of the intact skeleton of the human erythrocyte membrane.

1986 ◽  
Vol 102 (3) ◽  
pp. 997-1006 ◽  
Author(s):  
B W Shen ◽  
R Josephs ◽  
T L Steck
Keyword(s):  
Human Erythrocyte ◽  
Actin Filaments ◽  
Band 3 ◽  
Carbon Films ◽  
Erythrocyte Membranes ◽  
Accessory Proteins ◽  
Red Cell Membrane ◽  
Human Erythrocyte Membranes ◽  
Low Ionic Strength ◽  
Triton X

Filamentous skeletons were liberated from isolated human erythrocyte membranes in Triton X-100, spread on fenestrated carbon films, negatively stained, and viewed intact and unfixed in the transmission electron microscope. Two forms of the skeleton were examined: (a) basic skeletons, stripped of accessory proteins with 1.5 M NaCl so that they contain predominantly polypeptide bands 1, 2, 4.1, and 5; and (b) unstripped skeletons, which also bore accessory proteins such as ankyrin and band 3 and small plaques of residual lipid. Freshly prepared skeletons were highly condensed. Incubation at low ionic strength and in the presence of dithiothreitol for an hour or more caused an expansion of the skeletons, which greatly increased the visibility of their elements. The expansion may reflect the opening of spectrin from a compact to an elongated disposition. Expanded skeletons appeared to be organized as networks of short actin filaments joined by multiple (5-8) spectrin tetramers. In unstripped preparations, globular masses were observed near the centers of the spectrin filaments, probably corresponding to complexes of ankyrin with band 3 oligomers. Some of these globules linked pairs of spectrin filaments. Skeletons prepared with a minimum of perturbation had thickened actin protofilaments, presumably reflecting the presence of accessory proteins. The length of these actin filaments was highly uniform, averaging 33 +/- 5 nm. This is the length of nonmuscle tropomyosin. Since there is almost enough tropomyosin present to saturate the F-actin, our data support the hypothesis that tropomyosin may determine the length of actin protofilaments in the red cell membrane.

scholarly journals The aldolase-binding site of the human erythrocyte membrane is at the NH2 terminus of band 3.

1981 ◽  
Vol 256 (21) ◽  
pp. 11203-11208 ◽  
Author(s):  
S.N. Murthy ◽  
T. Liu ◽  
R.K. Kaul ◽  
H. Köhler ◽  
T.L. Steck
Keyword(s):  
Binding Site ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Band 3 ◽  
Human Erythrocyte Membrane

Isolation and Partial Structure of an Oligosaccharide of Band-3 Glycoproteins of Human Erythrocyte Membranes

1979 ◽  
pp. 1065-1072
Author(s):  
Toshiaki Osawa ◽  
Tsutomu Tsuji ◽  
Anne Marianne Golovtchenko-Matsumoto ◽  
Tatsuro Irimura
Keyword(s):  
Human Erythrocyte ◽  
Band 3 ◽  
Erythrocyte Membranes ◽  
Partial Structure ◽  
Human Erythrocyte Membranes

scholarly journals Three-dimensional map of the dimeric membrane domain of the human erythrocyte anion exchanger, Band 3.

1994 ◽  
Vol 13 (14) ◽  
pp. 3230-3235 ◽  
Author(s):  
D.N. Wang ◽  
V.E. Sarabia ◽  
R.A. Reithmeier ◽  
W. Kühlbrandt
Keyword(s):  
Anion Exchanger ◽  
Human Erythrocyte ◽  
Three Dimensional ◽  
Band 3 ◽  
Membrane Domain
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