Results 161 to 170 of about 8,155 (209)
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Carbonic anhydrase activity of erythrocyte ghosts

Experientia, 1968
Durch wiederholtes Waschen mit hypotonen Losungen gelingt es, mit dem Hamoglobin auch die Carboanhydrase vollstandig aus Erythrocytenstromata zu entfernen.
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Crosslinking of glycoproteins in human erythrocyte ghosts

Journal of Molecular Biology, 1974
Membrane glycoproteins of human erythrocytes can be resolved into three major bands (GP-1, GP-2, and GP-3) on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. When the ghosts or intact erythrocytes were reacted with a crosslinking reagent, dimethyl malonimidate, a novel glycoprotein band (GP-A) of crosslinked product appeared on gel ...
T H, Ji, I, Ji
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Retention of Potassium by Human Erythrocyte Ghosts

Nature, 1960
WHEN ghosts prepared from human erythrocytes by lysis in water are washed in a saline medium, sodium and potassium ions are nearly uniformly distributed across the ghost membranes1. In attempting to prepare ghosts with higher potassium and lower sodium concentrations than those of a saline medium we have found that incubation at 37° C.
J F, HOFFMAN, D C, TOSTESON, R, WHITTAM
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Spin probe clustering in human erythrocyte ghosts

The Journal of Membrane Biology, 1985
A model has been developed for 5-nitroxide stearate, I(12,3), distribution in human erythrocyte ghosts which accurately predicts ESR spectral alterations observed with increased probe/total lipid (P/L) at 37 degrees C. This spin probe occupies a class of high-affinity, noninteracting sites at low loading.
L M, Gordon, F D, Looney, C C, Curtain
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Preparation and properties of human erythrocyte ghosts

Molecular and Cellular Biochemistry, 1973
Ghosts are post-hemolytic residues of red blood cells. It is generally assumed that these residues are devoid of intracellular structure and consist primarily of the cell membrane. Hence ghosts are widely used in the study of composition, structure, and function of the red blood cell membrane.
Schwoch, G., Passow, H.
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Modification of human erythrocyte ghosts with transglutaminase

Biochemical and Biophysical Research Communications, 1975
Abstract Guinea pig liver transglutaminase was shown to catalyze the incorporation of dansylcadaverine and putrescine into two major protein fractions of human erythrocyte ghosts. As judged by sodium dodecylsulfate gel electrophoresis under reducing conditions, one of these is a high molecular weight polymer which may contain spectrin.
L, Lorand   +3 more
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Purine Phosphoribosyl Transferases in Human Erythrocyte Ghosts

1977
It is generally assumed that mammalian hypoxanthine-guanine phosphoribosyl transferase (HG-PRT; EC 2.4.2.8) and adenine phosphoribosyl transferase (A-PRT; EC 2.4.2.7) are soluble, cytoplasmic enzymes. All the isolation procedures for these enzymes are based on purification from cell free supernatant fractions (1–6).
C H, de Bruyn, T L, Oei
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Thiamin transport by human erythrocytes and ghosts

The Journal of Membrane Biology, 1990
Thiamin transport in human erythrocytes and resealed pink ghosts was evaluated by incubating both preparations at 37 or 20 degrees C in the presence of [3H]-thiamin of high specific activity. The rate of uptake was consistently higher in erythrocytes than in ghosts. In both preparations, the time course of uptake was independent from the presence of Na+
D, Casirola   +3 more
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An erythrocyte encapsulator dialyzer used in preparing large quantities of erythrocyte ghosts and encapsulation of a pesticide in erythrocyte ghosts

Analytical Biochemistry, 1980
Abstract An erythrocyte encapsulator dialyzer has been fabricated and tested for preparing large quantities of animal blood for encapsulation. Less than 25 min is required to dialyze 150 ml of erythrocytes for encapsulation. Data are presented showing ca 30% encapsulation of added substances for bovine, equine, and porcine erythrocytes. Encapsulation
J R, DeLoach, R L, Harris, G M, Ihler
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Cyclic AMP transport in human erythrocyte ghosts

Biochimica et Biophysica Acta (BBA) - Biomembranes, 1978
10(-5) M cyclic AMP has high permeability in human erythrocyte ghosts (p = 0.061-10(-6) cm.s-1). Saturation of influx and efflux occurs. Koizt = 4.43 mM. Voizt = 259.6 micron.min-1-Kiozt = 0.475 micron. Viozt = 28.3 micron.min-1 at 30 degrees C. Equilibrium exchange entry of cyclic AMP has similar kinetics to zero trans influx, though the system does ...
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