Results 191 to 200 of about 31,695 (232)
Some of the next articles are maybe not open access.
Electrophoresis of phosphoglycerate kinase
Biochemical Genetics, 1969A technique for the visualization of phosphoglycerate kinase on starch gel after electrophoresis is described. Three bands of activity were found in hemolysates prepared from normal red cells. When ATP, a substrate of the enzyme, was incorporated into the gel, only a single band was found.
openaire +2 more sources
Multiple forms of human phosphoglycerate kinase
Archives of Biochemistry and Biophysics, 1979Abstract Phosphoglycerate kinase was isolated by affinity chromatography from human skeletal muscle and erythrocytes. As in the tissue extracts, the purified enzyme showed in Cellogel electrophoresis one major and two minor bands with phosphoglycerate kinase activity. The multiple forms were separated by chromatography on CM-Sepharose. From the three
W K, Krietsch, I U, Freier, S W, Eber
openaire +2 more sources
The SH group of yeast phosphoglycerate kinase
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1973Abstract The single cysteine residue present in phosphoglycerate kinase (ATP:3-phospho- d -glycerate 1-phosphotransferase, EC 2.7.2.3) was modified with p- hydroxymercuribenzoate , N- ethylmaleimide , iodoacetate, iodoacetamide, and 5,5′-dithiobis-(2-nitrobenzoic acid).
L, Arvidsson, M, Larsson-Raźnikiewicz
openaire +2 more sources
Immunochemical studies on phosphoglycerate kinase deficiency
Biochemical Medicine and Metabolic Biology, 1986Antisera to normal erythrocyte and skeletal muscle PGK, raised in rabbits, were shown to cross-react with extracts from normal tissues and with extracts from a subject with PGK deficiency. Radial immunodiffusion, using the antisera raised against normal human PGK, was used to determine the amount of cross-reacting PGK protein present in extracts of ...
L G, Svirklys, W J, O'Sullivan
openaire +2 more sources
Configurational Distribution of Denatured Phosphoglycerate Kinase
Journal of Molecular Biology, 1993Physiochemical characterization of the denatured states of proteins is important for a complete understanding of the factors stabilizing their folded conformations. Using a combination of small angle neutron scattering (SANS), statistical mechanical modelling and molecular mechanics calculations, we examine the configurational distribution of ...
P, Calmettes +4 more
openaire +2 more sources
Phosphoglycerate Kinase Deficiency
2011Abstract This chapter provides pictures and clinical details of PHOSPHOGLYCERATE KINASE ...
Charles E. Schwartz +2 more
openaire +1 more source
Thermodynamic study of yeast phosphoglycerate kinase
Biochemistry, 1987Enthalpies of binding of MgADP, MgATP, and 3-phosphoglycerate to yeast phosphoglycerate kinase have been determined by flow calorimetry at 9.95-32.00 degrees C. Combination of these data with published dissociation constants [Scopes, R.K. (1978) Eur. J. Biochem.
C Q, Hu, J M, Sturtevant
openaire +2 more sources
Novel bisphosphonate inhibitors of phosphoglycerate kinase
Bioorganic & Medicinal Chemistry Letters, 1998A series of novel, conformationally-restrained bisphosphonate analogues of 1,3-bisphosphoglyceric acid 1 have been synthesised and evaluated as inhibitors of 3-PGK. They are competitive inhibitors of the human enzyme and, especially for certain alpha-halophosphonic acid analogues, both Ki and IC50 values extend into the submicromolar range.
N A, Caplan +3 more
openaire +2 more sources
X linkage of phosphoglycerate kinase in the mouse
Biochemical Genetics, 1974The levels of phosphoglycerate kinase (PGK), glucose 6-phosphate dehydrogenase (G6PD), and lactate dehydrogenase (LDH) were measured in one-cell embryos from X/0 and X/X females. Since the level of both PGK and G6PD was dependent on the number of X chromosomes present in the mother, these two enzymes are most likely coded for by X-linked genes.
Kozak, L P, McLean, G K, Eicher, E M
openaire +2 more sources
Structure of a circularly permuted phosphoglycerate kinase
Acta Crystallographica Section D Biological Crystallography, 2002The crystallographic structure of a circularly permuted form of yeast PGK, 72p yPGK, has been determined to a resolution of 2.3 A by molecular replacement. In this engineered protein, the C- and N-terminal residues of the wild-type protein are directly connected by a peptide bond and new N- and C-terminal residues are located within the N-terminal ...
Pierre, Tougard +4 more
openaire +2 more sources

