Phloretinyl-3'-benzylazide: a high affinity probe for the sugar transporter in human erythrocytes. II. Irreversible transport inhibition is induced by photolysis.

  title={Phloretinyl-3'-benzylazide: a high affinity probe for the sugar transporter in human erythrocytes. II. Irreversible transport inhibition is induced by photolysis.},
  author={Franklin F. Fannin and J. O. Evans and Donald F. Diedrich},
  journal={Biochimica et biophysica acta},
  volume={684 2},
In the dark, phloretinyl-3'-benzylazide (PBAz), at a nominal concentration of 10 microM, will inhibit the transport of D-glucose in human erythrocytes by more than 90%. This inhibition can be completely reversed by percolating the cell suspension through a small column of Sephadex G-10; cells recovered after this treatment, and then loaded with 100 mM D-glucose, possess a transport capacity (glucose efflux) equal to untreated cells. The Sephadex matrix completely removes non-covalently bound… Expand
5 Citations
Photoaffinity-labeling analogs of phlorizin and phloretin: synthesis and effects on cell membranes.
  • D. Diedrich
  • Chemistry, Medicine
  • Methods in enzymology
  • 1990
This chapter discusses the azides as membrane perturbants and photoaffinity-labeling agents and presents the results of an sodium dodecyl sulfate-polyacrylamide gel rod analysis of the radiolabeled membrane components from this experiment. Expand
Regulation of glucose transport by insulin and non-hormonal factors.
  • A. Klip
  • Biology, Medicine
  • Life sciences
  • 1982
An increase in the number of transport sites in the plasma membrane, due to incorporation of additional sites originating from intracellular membranes, has recently been proposed on the basis of both 3H-cytochalasin B binding and glucose transport determinations in isolated plasma and intraceocytes. Expand
Selective Covalent Modification of Membrane Components
Essential to an understanding of membrane-related biological phenomena at the molecular level is not only identification of the components involved but rather knowledge of their respective structuralExpand
Action of Drugs on the Erythrocyte Membrane
Drugs in the sense of pharmacologically active compounds have been important tools in the analysis of the structure and function of the erythrocyte (RBC) membrane. Conversely, the RBC membrane isExpand
Sugar transport in animal cells: the passive hexose transfer system.
  • A. Carruthers
  • Chemistry, Medicine
  • Progress in biophysics and molecular biology
  • 1984


Phloretinyl-3'-benzylazide: a high affinity probe for the sugar transporter in human erythrocytes. I. Hexose transport inhibition and photolabeling of mutarotase.
PBAz is a potentially useful photoaffinity labeling agent capable of covalently interacting with the transporter site facing the exterior of the red cell, making it one of the most effective reversible inhibitors known. Expand
The affinity of phlorizin-like compounds for a beta-glucosidase in intestinal brush borders: comparison with the glucose transport system.
The affinities of these compounds for the glucose transport system and phlorizin hydrolase were compared and the relative inhibitory potency of all but two of the analogs was the same in either system suggesting that there are similarities in the architecture of the two receptors. Expand
Maltosyl isothiocyanate: an affinity label for the glucose transporter of the human erythrocyte membrane. 1. Inhibition of glucose transport.
Kinetic analysis of glucose transport after treatment of erythrocytes with MITC revealed that VT was diminished while KT was unchanged, and transportable sugars and competitive inhibitors of monosaccharide transport protected against MITC inhibition, while carbohydrates which do not interact with the transporter gave no protection. Expand
Reconstitution of D-glucose transport in vesicles composed of lipids and intrinsic protein (zone 4.5) of the human erythrocyte membrane.
The stereospecificity and inhibition characteristics of the reconstituted transport imply that all the components of the erythrocyte D-glucose transport system are contained in the zone 4.5 membrane protein preparation. Expand
Binding of cytochalasin B to a red cell membrane protein.
  • S. Lin, J. Spudich
  • Biology, Medicine
  • Biochemical and biophysical research communications
  • 1974
This result and other observations suggest that the sugar transport-related cytochalasin B binding sites are most likely associated with the band 3 protein. Expand
The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes.
The effects of the ionic strength and pH of the hemolyzing solution on the hemoglobin content of human erythrocyte ghosts were studied in phosphate buffers and suggest an electrophysical interaction of hemoglobin with membrane constituents. Expand