Interaction of thiourea with band 3 in human red cell membranes

1985 ◽  
Vol 85 (1) ◽  
pp. 37-48 ◽  
Author(s):  
Peter L. Dorogi ◽  
A. K. Solomon
Keyword(s):  
Cell Membranes ◽  
Band 3 ◽  
Red Cell ◽  
Red Cell Membranes

Fine structure of the band 3 protein in human red cell membranes: Freeze-fracture studies

1978 ◽  
Vol 8 (3) ◽  
pp. 325-335 ◽  
Author(s):  
Ronald S. Weinstein ◽  
Jena K. Khodadad ◽  
Theodore L. Steck
Keyword(s):  
Fine Structure ◽  
Cell Membranes ◽  
Freeze Fracture ◽  
Band 3 ◽  
Red Cell ◽  
Band 3 Protein ◽  
Red Cell Membranes

Red Cell Membranes of Ankyrin-Deficientnb/nbMice Lack Band 3 Tetramers but Contain Normal Membrane Skeletons†

Biochemistry ◽  
1997 ◽  
Vol 36 (31) ◽  
pp. 9596-9604 ◽  
Author(s):  
Scott J. Yi ◽  
Shih-Chun Liu ◽  
Laura H. Derick ◽  
Murray ◽  
Jane E. Barker ◽  
...  
Keyword(s):  
Cell Membranes ◽  
Band 3 ◽  
Red Cell ◽  
Red Cell Membranes ◽  
Membrane Skeletons

Frequencies of Band 3 variants of human red cell membranes in some different populations

1990 ◽  
Vol 75 (2) ◽  
pp. 262-267 ◽  
Author(s):  
Helen M. Ranney ◽  
Gwen H. Rosenberg ◽  
Martin Morrison ◽  
Thomas J. Mueller
Keyword(s):  
Cell Membranes ◽  
Band 3 ◽  
Red Cell ◽  
Different Populations ◽  
Red Cell Membranes

scholarly journals Binding of Hemoglobin to Red Cell Membranes with Eosin-5-maleimide-Labeled Band 3:  Analysis of Centrifugation and Fluorescence Lifetime Data

Biochemistry ◽  
2002 ◽  
Vol 41 (27) ◽  
pp. 8630-8637 ◽  
Author(s):  
Afolorunso Andrew Demehin ◽  
Omoefe O. Abugo ◽  
Rajadas Jayakumar ◽  
Joseph R. Lakowicz ◽  
Joseph M. Rifkind
Keyword(s):  
Fluorescence Lifetime ◽  
Cell Membranes ◽  
Band 3 ◽  
Lifetime Data ◽  
Red Cell ◽  
Red Cell Membranes

BRIEF REPORT: Freeze-Cleaving of Red Cell Membranes in Paroxysmal Nocturnal Hemoglobinuria

Blood ◽  
1967 ◽  
Vol 30 (6) ◽  
pp. 785-791 ◽  
Author(s):  
RONALD S. WEINSTEIN ◽  
ROGER A. WILLIAMS
Keyword(s):  
Paroxysmal Nocturnal Hemoglobinuria ◽  
Cell Membranes ◽  
Red Cells ◽  
Red Cell ◽  
Electron Microscopic ◽  
Structural Differences ◽  
Microscopic Studies ◽  
Red Cell Membranes

Abstract Electron microscopic studies on dried isolated red cell ghosts have been reported to show lesions associated with cell membranes in paroxysmal nocturnal hemoglobinuria (PNH). In this study, carbon-platinum replicas of membranes of freeze-cleaved, partially hydrated PNH red cells and isolated PNH cell ghosts failed to confirm the existence of these abnormalities. This suggests that the previously described lesions are the products of drying artifacts, although they may reflect hidden structural differences between PNH and normal red cell membranes.

scholarly journals Temperature effects on sodium pump phosphoenzyme distribution in human red blood cells.

1985 ◽  
Vol 85 (1) ◽  
pp. 123-136 ◽  
Author(s):  
J H Kaplan ◽  
L J Kenney
Keyword(s):  
Atpase Activity ◽  
Cell Membranes ◽  
Conformational Transition ◽  
Fold Increase ◽  
Inhibitory Effect ◽  
Red Cell ◽  
Na Pump ◽  
Na Ions ◽  
Red Cell Membranes ◽  
Increasing Temperature

Phosphorylation of red cell membranes at ambient temperatures with micromolar [32P]ATP in the presence of Na ions produced phosphoenzyme that was dephosphorylated rapidly upon the addition of ADP or K ions. However, as first observed by Blostein (1968, J. Biol. Chem., 243:1957), the phosphoenzyme formed at 0 degrees C under otherwise identical conditions was insensitive to the addition of K ions but was dephosphorylated rapidly by ADP. This suggested that the conformational transition from ADP-sensitive, K-insensitive Na pump phosphoenzyme (E1 approximately P) to K-sensitive, ADP-insensitive phosphoenzyme (E2P) is blocked at 0 degrees C. Since the ATP:ADP exchange reaction is a partial reaction of the overall enzyme cycle dependent upon the steady state level of E1 approximately P that is regulated by [Na], we examined the effects of temperature on the curve relating [Na] to ouabain-sensitive ATP:ADP exchange. The characteristic triphasic curve seen at higher temperatures when [Na] was between 0.5 and 100 mM was not obtained at 0 degrees C. Simple saturation was observed instead with a K0.5 for Na of approximately 1 mM. The effect of increasing temperature on the ATP:ADP exchange at fixed (150 mM) Na was compared with the effect of increasing temperature on (Na + K)-ATPase activity of the same membrane preparation. It was observed that (a) at 0 degrees C, there was significant ouabain-sensitive ATP:ADP exchange activity, (b) at 0 degrees C, ouabain-sensitive (Na + K)-ATPase activity was virtually absent, and (c) in the temperature range 5-37 degrees C, there was an approximately 300-fold increase in (Na + K)-ATPase activity with only a 9-fold increase in the ATP:ADP exchange. These observations are in keeping with the suggestion that the E1 approximately P----E2P transition of the Na pump in human red cell membranes is blocked at 0 degrees C. Previous work has shown that the inhibitory effect of Na ions and the low-affinity stimulation by Na of the rate of ATP:ADP exchange occur at the extracellular surface of the Na pump. The absence of both of these effects at 0 degrees C, where E1 approximately P is maximal, supports the idea that external Na acts through sites on the E2P form of the phosphoenzyme.

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