Related ArticlesHypophosphite transport in human erythrocytes studied by overdetermined one-dimensional NMR exchange analysis.
NMR Biomed. 1990 Apr;3(2):59-63
Authors: Price WS, Kuchel PW
The membrane transport kinetics of the disubstituted phosphorus oxyacid, hypophosphite, were studied in human red cells under equilibrium exchange conditions. Hypophosphite is an analogue of both the bicarbonate and phosphate ions and is known to be rapidly transported across the human red cell membrane via the anion transport protein, Band 3. The hypophosphite ion is a particularly useful probe of Band 3-mediated membrane transport as the intracellular and extracellular species occur as distinct resonances in the 31P NMR spectrum; as a result the membrane potential may also be readily inferred. We applied 'overdetermined' one-dimensional exchange analysis to estimate the rates of exchange for influx and efflux. The apparent equilibrium exchange (ee) values Kmee for the hypophosphite efflux and influx were different and while the efflux parameters were not able to be unambiguously defined, the measured apparent influx kinetic transport parameters were Vmaxee = 1600 +/- 190 amol cell-1 s-1, and Kmee = 75 +/- 16 mM.
Role of aminotransferases in glutamate metabolism of human erythrocytes
Role of aminotransferases in glutamate metabolism of human erythrocytes
Abstract Human erythrocytes require a continual supply of glutamate to support glutathione synthesis, but are unable to transport this amino acid across their cell membrane. Consequently, erythrocytes rely on de novo glutamate biosynthesis from α-ketoglutarate and glutamine to maintain intracellular levels of glutamate. Erythrocytic glutamate biosynthesis is catalyzed by three enzymes, alanine aminotransferase (ALT), aspartate aminotransferase (AST), and glutamine aminohydrolase (GA). Although the presence of these...
nmrlearner
Journal club
0
03-09-2011 04:19 AM
[NMR paper] 13C/31P NMR studies on the role of glucose transport/phosphorylation in human glycoge
13C/31P NMR studies on the role of glucose transport/phosphorylation in human glycogen supercompensation.
Related Articles 13C/31P NMR studies on the role of glucose transport/phosphorylation in human glycogen supercompensation.
Int J Sports Med. 2003 May;24(4):238-44
Authors: Price TB, Laurent D, Petersen KF
This study measured muscle glycogen during a 7-day carbohydrate loading protocol. Twenty healthy subjects (12 male, 8 female) performed 1 hr treadmill/toe-raise exercise immediately before a 3-day low carbohydrate (LoCHO) diet (20 %...
nmrlearner
Journal club
0
11-24-2010 09:01 PM
[NMR paper] Backbone dynamics of the human MIA protein studied by (15)N NMR relaxation: implicati
Backbone dynamics of the human MIA protein studied by (15)N NMR relaxation: implications for extended interactions of SH3 domains.
Related Articles Backbone dynamics of the human MIA protein studied by (15)N NMR relaxation: implications for extended interactions of SH3 domains.
Protein Sci. 2003 Mar;12(3):510-9
Authors: Stoll R, Renner C, Buettner R, Voelter W, Bosserhoff AK, Holak TA
The melanoma inhibitory activity (MIA) protein is a clinically valuable marker in patients with malignant melanoma as enhanced values diagnose metastatic...
nmrlearner
Journal club
0
11-24-2010 09:01 PM
[NMR paper] Galactose metabolism in normal human lymphoblasts studied by (1)H, (13)C and (31)P NM
Galactose metabolism in normal human lymphoblasts studied by (1)H, (13)C and (31)P NMR spectroscopy of extracts.
Related Articles Galactose metabolism in normal human lymphoblasts studied by (1)H, (13)C and (31)P NMR spectroscopy of extracts.
NMR Biomed. 2001 May;14(3):192-8
Authors: Wehrli SL, Reynolds R, Chen J, Yager C, Segal S
The development of tools to follow and quantitate the fate of galactose in mammalian cells is crucial to the study and understanding of the inherited disorders of galactose metabolism. In this study we incubated...
nmrlearner
Journal club
0
11-19-2010 08:32 PM
[NMR paper] Weak substrate binding to transport proteins studied by NMR.
Weak substrate binding to transport proteins studied by NMR.
Related Articles Weak substrate binding to transport proteins studied by NMR.
Biophys J. 1998 Dec;75(6):2794-800
Authors: Spooner PJ, O'Reilly WJ, Homans SW, Rutherford NG, Henderson PJ, Watts A
The weak binding of sugar substrates fails to induce any quantifiable physical changes in the L-fucose-H+ symport protein, FucP, from Escherichia coli, and this protein lacks any strongly binding ligands for competitive binding assays. Access to substrate binding behavior is however possible...
nmrlearner
Journal club
0
11-17-2010 11:15 PM
[NMR paper] Kinetics of choline transport and phosphorylation in human breast cancer cells; NMR a
Kinetics of choline transport and phosphorylation in human breast cancer cells; NMR application of the zero trans method.
Related Articles Kinetics of choline transport and phosphorylation in human breast cancer cells; NMR application of the zero trans method.
Anticancer Res. 1996 May-Jun;16(3B):1375-80
Authors: Katz-Brull R, Degani H
The mechanism and kinetics of choline transport and phosphorylation in MCF7 human breast cancer cells was studied by 31P, 13C and 2H NMR, applying the zero trans method. Choline was transported by a...
nmrlearner
Journal club
0
08-22-2010 02:27 PM
[NMR paper] 7Li NMR relaxation study of Li+ binding in human erythrocytes.
7Li NMR relaxation study of Li+ binding in human erythrocytes.
Related Articles 7Li NMR relaxation study of Li+ binding in human erythrocytes.
Biochemistry. 1993 Dec 14;32(49):13490-8
Authors: Rong Q, Espanol M, Mota de Freitas D, Geraldes CF
We used 7Li NMR spin-lattice (T1) and spin-spin (T2) relaxation time measurements to investigate the binding of Li+ in human red blood cell (RBC) suspensions. In RBCs containing 1.4 mM Li+, the intracellular 7Li NMR T2 relaxation value (0.30 +/- 0.03 s) was much smaller than the corresponding T1 value...
nmrlearner
Journal club
0
08-22-2010 03:01 AM
[NMR paper] Structure-function relationships in human epidermal growth factor studied by site-dir
Structure-function relationships in human epidermal growth factor studied by site-directed mutagenesis and 1H NMR.
Related Articles Structure-function relationships in human epidermal growth factor studied by site-directed mutagenesis and 1H NMR.
Biochemistry. 1991 Sep 10;30(36):8891-8
Authors: Hommel U, Dudgeon TJ, Fallon A, Edwards RM, Campbell ID
In order to elucidate the mechanism of interaction between human epidermal growth factor (EGF) and its receptor, selected variants of EGF, differing by single amino acid substitutions, have been...