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Evidence for a pool of non-recycling transferrin receptors in peripheral sheep reticulocytes

โœ Scribed by M. Adam; C. Wu; C. Turbide; J. Larrick; R. M. Johnstone


Book ID
102881592
Publisher
John Wiley and Sons
Year
1986
Tongue
English
Weight
1006 KB
Volume
127
Category
Article
ISSN
0021-9541

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โœฆ Synopsis


Sheep reticulocytes from phlebotomized animals have a total transferrin binding potential that may exceed by an order of magnitude the surface binding capacity. Steady state uptake of transferrin at 37 degrees C is generally less than 50% of the total transferrin binding capacity. During long-term incubation of the reticulocytes, all transferrin binding ability is lost, the ability to internalize being lost most rapidly. The loss in ability to bind transferrin during long-term incubation is independent of the number of surface transferrin binding sites, since removal of surface receptors with pronase does not affect the rate of loss of the internal pool of receptors during long-term incubation. Moreover, after removing surface receptors with pronase, only a fraction of the original number of receptors is restored to the surface, despite the presence of a large pool of internal receptors. These data suggest that only a fraction of the internal pool of receptors is capable of recycling to the cell surface in sheep reticulocytes.


๐Ÿ“œ SIMILAR VOLUMES


Electron microscopic evidence for extern
โœ Pan, Bin Tao (author);Teng, Kathy (author);Wu, Choan (author);Adam, Mohammed (au ๐Ÿ“‚ Article ๐Ÿ“… 1985 ๐Ÿ› Rockefeller University Press. ๐ŸŒ English โš– 937 KB

Using ferritin-labeled protein A and colloidal gold-labeled anti-rabbit IgG, the fate of the sheep transferrin receptor has been followed microscopically during reticulocyte maturation in vitro. After a few minutes of incubation at 37 degrees C, the receptor is found on the cell surface or in simple