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Receptor-mediated endocytosis of transferrin in K562 cells.
Human diferric transferrin binds to the surface of K562 cells, a human leukemic cell line. There are about 1.6 X 10(5) binding sites per cell surface, exhibiting a KD of about 10(-9) M. Upon warmingExpand
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Binding of apotransferrin to K562 cells: explanation of the transferrin cycle.
The binding of apotransferrin to the transferrin receptor on the surface of human leukemic K562 cells was found to be significantly less tight than that of the holoprotein, diferric transferrin. TheExpand
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Receptor-mediated endocytosis of transferrin and the uptake of fe in K562 cells: identification of a nonlysosomal acidic compartment.
At physiological temperature, the Fe-carrier transferrin is taken up by K562 human erythroleukemia cells through receptor-mediated endocytosis. Both ligand (now minus Fe) and receptor recycle back toExpand
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Rapid internalization of the transferrin receptor in K562 cells is triggered by ligand binding or treatment with a phorbol ester.
Treatment of human K562 cells with 4 beta-phorbol 12-myristate 13-acetate (PMA) resulted in an approximately 50% reduction in cell surface transferrin receptors within 30-45 min as judged by bindingExpand
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Reconstitution of membrane proteins.
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The nuclear matrix from cells of different origin. Evidence for a common set of matrix proteins.
We compared the protein composition of the nuclear matrix isolated from several murine embryonal carcinoma cells and mature tissues by two-dimensional gel electrophoresis. Two nuclear matrixExpand
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Failure to release iron from transferrin in a Chinese hamster ovary cell mutant pleiotropically defective in endocytosis
A Chinese hamster ovary cell mutant defective in the receptor-mediated endocytosis of several unrelated ligands (Robbins, A. R., S. S. Peng, and J. L. Marshall, 1983, J. Cell Biol., 96:1064-1071)Expand
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The folding of ovalbumin. Renaturation in vitro versus biosynthesis in vitro.
Hen ovalbumin, the major secretory product of oviduct cells, is a 43 000-dalton glycoprotein. Many studies have led to controversy over the question of whether ovalbumin (OA) can be fully renaturedExpand
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Voltage-dependent trans-bilayer orientation of melittin.
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Separation of Fe+3 from transferrin in endocytosis
NH4Cl and monensin, two agents which neutralize intracellular acidic compartments, block the segregation of iron from transferrin after endocytosis, while neither of these reagents affectsExpand
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