Cytochalasin B binding sites and glucose transport carrier in human erythrocyte ghosts.
نویسندگان
چکیده
منابع مشابه
Glucose Transport Carrier in Human Erythrocyte Membranes
The effect of D-glucose on dinitrophenylation of membrane proteins of human erythrocyte ghosts by I-fluoro-2,4-dinltrobenzene was studied in the absence and in the presence of D-glucose. A double isotopic, differential labeling technique followed by gel electrophoresis of extracts in the presence of sodium dodecyl sulfate revealed the presence of a polypeptide, or polypeptides, in human erythro...
متن کاملActive Calcium and Strontium Transport in Human Erythrocyte Ghosts
Both calcium and strontium could be transported actively from erythrocytes if adenosine triphosphate, guanosine triphosphate, or inosine triphosphate were included in the hypotonic medium used to infuse calcium or strontium into the cells. Acetyl phosphate and pyrophosphate were not energy sources for the transport of either ion. Neither calcium nor strontium transport was accompanied by magnes...
متن کاملOrganic-acid transport in resealed haemoglobin-containing human erythrocyte 'ghosts'.
The transport of organic acids across the membrane of resealed haemoglobin-containing erythrocyte 'ghosts' prepared by a dialysis technique has been studied. The present work forms part of studies directed towards the use of erythrocyte cellular carriers in enzyme-replacement therapy of inherited metabolic diseases. Oxalic acid, glycollic acid and glyoxylic acid were taken as representative of ...
متن کاملStimulation of 32Pi transport into human erythrocyte ghosts and reconstituted vesicles by Mg2+ and hemoglobin.
Human erythrocyte ghosts catalyze a low rate of 32Pi uptake. A severalfold stimulation of 32Pi uptake was observed after exposure of the membranes to an erythrocyte lysate or to hemoglobin in the presence of Mg2+. Ghosts prepared from erythrocytes that had been exposed to 10 microM 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid showed a marked reduction in 32Pi uptake. Reconstitution of membr...
متن کاملActive transport of GSSG from reconstituted erythrocyte ghosts.
Human erythrocyte ghosts were loaded with 35S-labeled GSSG and with a sucrose marker, and the transport of GSSG to the suspending medium was studied. GSSG transport from ghosts occurred only when ATP was also present in the ghosts, proceeded against a concentration gradient, and was inhibited by fluoride. The rate of transport was dependent upon the intracellular concentration of GSSG. The rela...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1977
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)63372-7