Abstract
The monosaccharide transport system of the human erythrocyte. Solubilization and characterization on the basis of cytochalasin B binding.
Highlights
The monosaccharide transport system of the human erythrocyte has been characterized by means of its affinity for cytochalasin B
Previous studies have shown that intact erythrocyte membranes have two (Lin and Snyder, 1977) or three (Jung and Rampal, 1977) types of high affinity sites for cytochalasin B
(Fig. l), and the data for the binding of cytochalasin B are adequately described by a scheme that assumes only these high affinity sites exist in the protein-depleted membranes (Figs. 1 and 2)
Summary
The monosaccharide transport system of the human erythrocyte has been characterized by means of its affinity for cytochalasin B. The detergent-solubilized complex was assayed by first removing the Triton with polystyrene beads and measuring the binding of cytochalasin B by equilibrium dialysis. Since we have not measured the transport function per se, we employ the term “cytochalasin B binding complex” rather than “monosaccharide transport system.” By means of this assay, the extent of solubilization of the complex with Triton X-100 has been quantitatively described. It has been possible to estimate the size and protein content of the complex in detergent through a combination of molecular exclusion chromatography and sucrose gradient centrifugation in Hz0 and D20 These separation procedures have given information about identity of the polypeptide(s) in the complex. The effect of Triton solubilization on the affinities of the complex for cytochalasin B and D-glucose has been examined
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
