Results 271 to 280 of about 90,505 (292)
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Molecular and Cellular Biochemistry, 1981
Several metabolic compounds have been found to be competitive inhibitors of the anomerase activity of phosphoglucose isomerase (EC 5.3.1.9).Ki values for erythrose 4-phosphate, 6-phosphogluconate, and fructose 1,6-bisphosphate for the anomerase reaction are 0.32 muM, 21 muM, and 84 muM respectively at 0 degree and pH 8.2.
Keith J. Schray +1 more
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Several metabolic compounds have been found to be competitive inhibitors of the anomerase activity of phosphoglucose isomerase (EC 5.3.1.9).Ki values for erythrose 4-phosphate, 6-phosphogluconate, and fructose 1,6-bisphosphate for the anomerase reaction are 0.32 muM, 21 muM, and 84 muM respectively at 0 degree and pH 8.2.
Keith J. Schray +1 more
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Isomerase and Chaperone Activity of Prolyl Isomerase in the Folding of Carbonic Anhydrase
Science, 1992Several proteins have been discovered that either catalyze slow protein-folding reactions or assist folding in the cell. Prolyl isomerase, which has been shown to accelerate rate-limiting cis-trans peptidyl-proline isomerization steps in the folding pathway, can also participate in the protein-folding process as a ...
Nils Bergenhem +4 more
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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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Periplasmic Chaperones and Prolyl Isomerases
EcoSal Plus, 2018The biogenesis of periplasmic and outer membrane proteins (OMPs) in Escherichia coli is assisted by a variety of processes that help with their folding and transport to their final destination in the cellular envelope.
Stull, Frederick +2 more
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Thermoinactivation mechanism of glucose isomerase
Applied Biochemistry and Biotechnology, 2007In this article, the mechanisms of thermoinactivation of glucose isomerase (GI) from Streptomyces rubiginosus (in soluble and immobilized forms) were investigated, particularly the contributions of thiol oxidation of the enzyme's cysteine residue and a "Maillard-like" reaction between the enzyme and sugars in high fructose corn syrup (HFCS). Soluble GI
Bradley A. Saville, Leng Hong Lim
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Reactions of purified tissue phosphohexose isomerases with liver phosphohexose isomerase antiserum
Archives of Biochemistry and Biophysics, 1959Abstract Purified phosphohexose isomerases were prepared from tissues of dog, man, rabbit, and rat; antisera against human and dog liver isomerases were prepared in the rabbit. Inhibition of liver phosphohexose isomerase by its antiserum was uncompetitive with respect to substrate. The enzyme was completely precipitated by antiserum within 4 hr. from
Oscar Bodansky +2 more
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[97] Bacterial ribosephosphate isomerase
1982Publisher Summary This chapter discusses the several assay procedures available for detecting ribosephosphate isomerase activity. Ribosephosphate isomerase (RPI) catalyzes the interconversion of D-ribose 5-phosphate and ribulose 5-phosphate. The enzyme is found in both heterotrophic and autotrophic bacteria and its perceived role in metabolism ...
C.R. Middaugh, R.D. MacElroy
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1982
Publisher Summary This chapter describes the assay method, purification, and properties of D-ribose isomerase. The amount of ketose, D-ribulose, formed from D-ribose is determined by the cysteine-carbazole method. The D-ribose isomerase is an inducible enzyme and it is necessary to culture the bacteria in a medium containing D-ribose.
Ken Izumori, Alan D. Elbein
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Publisher Summary This chapter describes the assay method, purification, and properties of D-ribose isomerase. The amount of ketose, D-ribulose, formed from D-ribose is determined by the cysteine-carbazole method. The D-ribose isomerase is an inducible enzyme and it is necessary to culture the bacteria in a medium containing D-ribose.
Ken Izumori, Alan D. Elbein
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[38] Protein disulfide-isomerase
1995Publisher Summary Protein disulfide-isomerase is an abundant protein within the lumen of the endoplasmic reticulum of secretory cells, and functions as a catalyst in the formation of native disulfide bonds in nascent secretory and cell surface proteins.
Hilary C. Hawkins +2 more
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Serum Phosphoexose Isomerase in Cancer
Tumori Journal, 1977Serum levels of phosphoexose isomerase (PHI) were determined in 138 cancer patients. The enzyme levels showed a relation to the clinical stage of the tumor, and were, on the average, higher in advanced disease. The behavior of the enzyme levels after chemotherapy and/or radiotherapy was studied in relation to the clinical response.
Ettore Cunietti, Maura Greco
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