Results 201 to 210 of about 18,060 (230)
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The determination of triosephosphate isomerase
Archives of Biochemistry and Biophysics, 1956Abstract The difference in rate of formation of the chromogenic 2,4-dinitrophenylosazone derivatives of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate permits accurate measurement of the two triose phosphates in a mixture by means of carefully timed chromogen development reactions.
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Immobilized triosephosphate isomerases a comparative study
Applied Biochemistry and Biotechnology, 1992Pig muscle triosephosphate isomerase was covalently attached to polyacrylamide and silica-based supports possessing carboxylic or aldehyde functional groups or activated with p-benzoquinone. A silica-based support activated with p-benzoquinone proved to be the most advantageous. There were no profound alterations in the catalytic properties as a result
M, Abrahám, A, Alexin, B, Szajáni
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Removal of Triosephosphate, Isomerase from Albumins
Preparative Biochemistry, 1973Abstract Commercial serum albumin and ovalbumin from a variety of sources contain triosephosphate isomerase activity which can interfere with many enzyme assays and metabolic studies. A simple procedure is described for the removal of this contaminant by preparative electrophoresis or electrofocus-ing.
D W, Porter, B G, Harris, R W, Gracy
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Triosephosphate Isomerase Deficiency: Predictions and Facts
Journal of Theoretical Biology, 1996Deficiencies in around 20 enzymes, associated with widely different degrees of severity and complexity, have been identified for human erythrocytes. The fact that glycolysis is crucial for erythrocyte function is reflected by the large number of inherited glycolytic enzymopathies. Triosephosphate isomerase (TPI) deficiency, a rare autosomal disease, is
F, Orosz +4 more
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The Folding Pathway of Triosephosphate Isomerase
2008Publisher Summary This chapter discusses the folding pathway of triosephosphate isomerase (TIM), which is a widely studied enzyme. The ubiquity, efficient catalytic activity, and (β/α)8 barrel three-dimensional conformation of this enzyme makes it an excellent model to perform almost any kind of research. TIM is a glycolytic enzyme that catalyzes the
Francisco, Zárate-Pérez +2 more
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Triosephosphate isomerase: a highly evolved biocatalyst
Cellular and Molecular Life Sciences, 2010Triosephosphate isomerase (TIM) is a perfectly evolved enzyme which very fast interconverts dihydroxyacetone phosphate and D: -glyceraldehyde-3-phosphate. Its catalytic site is at the dimer interface, but the four catalytic residues, Asn11, Lys13, His95 and Glu167, are from the same subunit. Glu167 is the catalytic base. An important feature of the TIM
R K, Wierenga +2 more
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Allosteric properties of rabbit triosephosphate isomerase
Life Sciences, 1971Abstract Rabbit triosephosphate isomerase, except for the occurence of substrate inhibition, obeys the simple Michaelis-Menton equation with glyceraldehyde-3-phosphate as substrate. But with dihydroxycetone phosphate as substrate, it exhibits sigmoidal kinetics. Its isomerase activity can be inhibited by various phosphates and metabolites.
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Detection of Triosephosphate Isomerase after Electrophoresis
Nature, 1964BY coupling enzymes to the reduction of a tetrazolium salt, dehydrogenases can be located on electrophoresis strips, and several have been shown to consist of more than one protein component1,2. It is possible to detect other enzymes if their action leads to the formation of a compound which can be oxidized by a suitable enzyme in the incubation ...
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In vitro deamidation of human triosephosphate isomerase
Archives of Biochemistry and Biophysics, 1986The effects of pH, temperature, buffer ion, ionic strength, protein concentration, and substrate on the rates of specific, spontaneous deamidations of Asn-15 and Asn-71 of human triosephosphate isomerase were examined. Elevated temperature and pH facilitate the deamidations, and the deamidation rate is dependent on the specific buffer ions indicating a
K U, Yüksel, R W, Gracy
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Triosephosphate isomerase from selected chlorophyta
Phytochemistry, 1968Abstract The triosephosphate isomerase systems from two algal species, Ankistrodesmus Braunii and Scenedesmus acuminatus , have been isolated and partially purified by a series of solvent and salt fractionations. The enzymes from A. Braunii and S. acuminatus were electrophoretically homogeneous with uncorrected mobilities of −1·2 × 10 −5 cm 2
J.C. Meeks, D.L. Willson, R.D. Gaines
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