Human Erythrocyte Sugar Transport
Journal of Biological ChemistryPublished 1 March 1974Open access
Robert J. Bloch
Citations44
SJR quartileQ1
SJR score1.71
SNIP1.00
Generate an AI Snapshot to get a quick, structured summary of this paper.
Study Snapshot
ObjectiveStudy objective
MethodsResearch methodology
PopulationPopulation studied
Sample sizeSample sizes
OutcomesStudy outcomes here
ResultsStudy results comes here
LimitationsResearch study limitations comes here
A concise AI-generated summary of the paper will appear here once you click Generate AI Snapshot.
TL;DR
Inhibition of transport by sodium tetrathionate and iodoacetamide are due to modification of a sulfhydryl group, and 1-Fluoro-2,4-dinitrobenzene and N-ethylmaleimide inhibit transport by reacting with an amino group.
Abstract
Abstract Human erythrocytes were reacted with several compounds in an attempt to identify the residues essential for sugar transport. Inhibition of transport by sodium tetrathionate and iodoacetamide are due to modification of a sulfhydryl group. 1-Fluoro-2,4-dinitrobenzene and N-ethylmaleimide inhibit transport by reacting with an amino group. Studies with 5-dimethylaminonaphthalene-1-sulfonyl chloride and rose bengal indicate that a third group, probably an imidazole, is also required for activity. Various aspects of modification with these reagents were studied in an effort to assign these groups specific roles in the transport process.
Keywords
MedicineBiochemistry, Genetics and Molecular Biology
Analytical ChemistryAutomatic Recording Apparatus for Use in Chromatography of Amino Acids
9,593 Citations1958D. Spackman, William H. Stein +1 more
Archives of Biochemistry and BiophysicsThe preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes
4,417 Citations1963James T. Dodge, Carolyn D. Mitchell +1 more
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.
BiochemistryTetranitromethane. A Reagent for the Nitration of Tyrosyl Residues in Proteins<sup>*</sup>
635 Citations1966Mordechai Sokolovsky, James Riordan +1 more
The Journal of General PhysiologyLocalization of Erythrocyte Membrane Sulfhydryl Groups Essential for Glucose Transport
298 Citations1965John VanSteveninck, Robert I. Weed +1 more
With chlormerodrin and PCMBS it was demonstrated that the inhibition results from interactions with the sulfhydryl groups located on the outer surface of the membrane, capable of inhibiting glucose transport in the red cell.
The Journal of PhysiologyDetermination of the temperature and pH dependence of glucose transfer across the human erythrocyte membrane measured by glucose exit
263 Citations1962Arindam Sen, W. F. Widdas
The Journal of General PhysiologyEVIDENCE OF ACTIVE TRANSFER OF CERTAIN NON-ELECTROLYTES ACROSS THE HUMAN RED CELL MEMBRANE
198 Citations1948Paul G. LeFevre
The intermediation of a sulfhydryl group at the cell surface, probably an enzymatic phosphorylation, is suggested as an essential step in the passage of glycerol, glucose, and other like substances, across the human red cell membrane.
BiochemistryPhotooxidation with Rose Bengal of a Critical Histidine Residue in Yeast Enolase<sup>*</sup>
193 Citations1965Edward W. Westhead
Biochemical and Biophysical Research CommunicationsThiolysis of some dinitrophenyl derivatives of amino acids
166 Citations1967Shmuel Shaltiel
This paper describes a method for quantitative removal of dinitrophenyl groups from histidine, tyrosine and cysteine side chains using FDNB, a reactive aryl halide that may find a variety of applications in peptide and protein chemistry.
Journal of the American Chemical SocietyAN ALBUMIN FRACTION ISOLATED FROM HUMAN PLASMA AS A CRYSTALLINE MERCURIC SALT
160 Citations1947Walter L. Hughes
BiochemistryThe Reaction of Diazonium-1H-tetrazole with Proteins. Determination of Tyrosine and Histidine Content<sup>*</sup>
118 Citations1966Mordechai Sokolovsky, Bert L. Vallée
The Journal of General PhysiologyTracer Exchange <i>vs</i>. Net Uptake of Glucose through Human Red Cell Surface
103 Citations1960Paul G. LeFevre, G. F. McGinniss
The speeds of gross chemical equilibration and of tracer glucose Equilibration were compared by means of serial analyses on quickly separated cells and media, in thick red cell suspensions, and the comparative rates observed are predicted by the previously proposed facilitated-diffusion mobile-carrier model for monosaccharide transfer.
BiochemistryEvidence for a carrier conformational change associated with sugar transport in erythrocytes
99 Citations1971R. M. Krupka
The Journal of PhysiologyThe action of inhibitors on the facilitated hexose transfer system in erythrocytes
95 Citations1958Freda Bowyer, W. F. Widdas
Archives of Biochemistry and BiophysicsInfluence of dye binding on the sensitized photooxidation of amino acids
89 Citations1968Judith S. Bellin, C.A. Yankus
The kinetics of the photooxidation of histidine sensitized by both rose bengal and methylene blue agree with those observed for the proflavin-sensitized autooxidation for p -toluene diamine.
Biochimica et Biophysica Acta (BBA) - Reviews on BiomembranesCarrier and non-carrier models for sugar transport in the human red blood cell
83 Citations1972W.R. Lieb, Wilfred D. Stein
Biochimica et Biophysica Acta (BBA) - EnzymologySite actif des ATP: Guanidine phosphotransférases
77 Citations1968Ridha Kassab, Claude Roustan +1 more
High voltage electrophoresis and thin-layer chromatography of the single fluorescent derivative isolated after pronase digestion of the dansylated enzymes led to the identification of e-DNS-lysine; these data provide evidence that the residue affected in both proteins is a lysine side chain.
The Journal of PhysiologyVariations of the parameters of glucose transfer across the human erythrocyte membrane in the presence of inhibitors of transfer
73 Citations1962Arindam Sen, W. F. Widdas
In a previous paper (Sen & Widdas, 1962), a method of determining the parameters of the glucose transfer system in erythrocytes was described, and it was hoped that inhibitor studies might give further evidence on the magnitude of the half-saturation concentration for glucose.
Journal of Biological ChemistryDemonstration of the Presence of a Histidine Residue at the Active Site of Streptococcal Proteinase
62 Citations1967Teh‐Yung Liu
Direct chemical evidence is furnished for the involvement of a histidine residue, as well as of a sulfhydryl group, in the active site of streptococcal proteinase.
Journal of Biological ChemistryAn Essential Histidine in the Catalytic Activities of 3-Phosphoglyceraldehyde Dehydrogenase
61 Citations1970Judith Bond, Sharron H. Francis +1 more
The effects of photooxidation produced a permanent change in the enzyme whereas the dark inhibitions were completely reversed by removal of the dye from the enzyme surface with charcoal treatment.
European Journal of BiochemistryReactivity of Sulfhydryl Groups in Micelles
60 Citations1968P. Heitmann
The observed effects on the apparent second-order rate constants related to the total concentration of mercapto compound are even higher, since the degree of SH ionization is greater in the eationic micelle than in the bulk phase, while the magnitude of the latter effect decreases strongly with addition of other electrolytes to the medium.
The Journal of PhysiologyInhibition of the glucose permeability of human erythrocytes by <i>N</i>‐ethyl maleimide
51 Citations1963Ann C. Dawson, W. F. Widdas
P peculiarities of the reaction have thrown further light on the factors involved in this type of inhibition and may be of value in the elucidation of the biochemical nature of the membrane component.
Methods in enzymology on CD-ROM/Methods in enzymology[32] Dye-sensitized photooxidation
47 Citations1972Edward W. Westhead
This chapter presents a technique, dye-sensitized photooxidation of enzymes for identification of critical residues at the catalytic site, and indicates that for some enzymes and under some circumstances, the method can indeed be a useful tool for tile determination of mechanisms or functional groups.
BiochemistryInhibition of sugar transport in erythrocytes by fluorodinitrobenzene
42 Citations1971R. M. Krupka
Discussions of the Faraday SocietyThe facilitated transfer of glucose and related compounds across the erythrocyte membrane
40 Citations1956Freda Bowyer, W. F. Widdas
Journal of Biological ChemistryCrystalline Papain Derivative Containing an Intramolecular Mercury Bridge
38 Citations1969Ruth Arnon, Emmanuel Shapira
Pap·2Hg is enzymatically active on a range of substrates; in respect to the hydrolysis of benzoyl-l-arginine ethyl ester its Vmax is similar to that of native papain, but its Km value is 0.042 compared to a value of 0.023 obtained fornative papain.
BiochemistryDinitrophenylation and thiolysis in the reversible labeling of a cysteine residue associated with the nicotinamide adenine dinucleotide site of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase
36 Citations1969Shmuel Shaltiel, Marco R. Soria
Journal of Biological ChemistryThe Dinitrophenylation of Human Carbonic Anhydrase B
15 Citations1971Pierre A. Henkart, Friedrich Dorner
Analysis of the tryptic peptides of dinitrophenyl carbonic anhydrase shows that reaction takes place with histidine residue 204, the same residue modified by iodoacetate, which is suggested that histidine 204, while clearly in the active site, may not play any direct role in enzyme catalysis.
Biochimica et Biophysica Acta (BBA) - BiomembranesThe influence of analogues of i-fluoro-2,4-dinitrobenzene on the kinetics of irreversible inhibition of sugar transport in the human erythrocyte
5 Citations1970E. R. A. Shimmin, Wilfred D. Stein
A mechanism for inhibition of the transport system by 1-fluoro-2,4-dinitrobenzene is proposed and it is proposed that the kinetics to a pseudo-unimolecular form in the presence of inhibitor is proposed.
Biochemical and Biophysical Research CommunicationsProperties of the active center histidine of α-chymotrypsin
4 Citations1972W.H. Cruickshank, Harvey Kaplan
Data supports the proposal that a charge relay mechanism is operative in chymotrypsin catalysis above pH 8 and shows that the system responsible for this mechanism is disrupted in the free enzyme.