Enzyme Characterization
Mostrando 1-12 de 3750 artigos, teses e dissertações.
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1. Characterization of a Small Proteolytic Enzyme Which Lyses Bacterial Cell Walls
Ensign, J. C. (University of Wisconsin, Madison), and R. S. Wolfe. Characterization of a small proteolytic enzyme which lyses bacterial cell walls. J. Bacteriol. 91:524–534. 1966.—An enzyme isolated from a myxobacter possesses both cell-wall lytic and proteolytic activity. The enzyme has been purified over 600-fold and is electrophoretically homogeneous
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2. Purification and characterization of selenocysteine beta-lyase from Citrobacter freundii.
The purification and characterization of bacterial selenocysteine beta-lyase, an enzyme which specifically catalyzes the cleavage of L-selenocysteine to L-alanine and Se0, are presented. The enzyme, purified to near homogeneity from Citrobacter freundii, is monomeric with a molecular weight of ca. 64,000 and contains 1 mol of pyridoxal 5'-phosphate as a cofa
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3. The Blue Copper-Containing Nitrite Reductase from Alcaligenes xylosoxidans: Cloning of the nirA Gene and Characterization of the Recombinant Enzyme
The nirA gene encoding the blue dissimilatory nitrite reductase from Alcaligenes xylosoxidans has been cloned and sequenced. To our knowledge, this is the first report of the characterization of a gene encoding a blue copper-containing nitrite reductase. The deduced amino acid sequence exhibits a high degree of similarity to other copper-containing nitrite r
American Society for Microbiology.
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4. Isolation and characterization of an enzyme with esterase activity from Micropolyspora faeni.
The isolation and the characterization of one of the enzymes of Micropolyspora faeni that hydrolyzes the substrate N-benzoyl-DL-phenylalanine-beta-naphthyl ester and that seems to be of medical importance are described. This enzyme (enzyme 1) was isolated with an 86-fold purification by using the following seven steps: ammonium sulfate precipitation, gel fil
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5. Genetic and biochemical characterization of D-arabinose dehydrogenase from Neurospora crassa.
D-Arabinose dehydrogenase has been purified to homogeneity from wild-type Neurospora crassa 74-A (FGSC 262) and from two colonial mutants, col-15a (FGSC 1391) and col-16a (FGSC 1349), found to contain more of the enzyme. The enzymes were characterized by measurement of several kinetic and physicochemical parameters. The enzymes were the same in all character
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6. Imobilização de uma β-galactosidase produzida por Kluyveromyces lactis NRRL Y-1564 cultivada em soro de leite.
Repositório Institucional da Universidade Federal do Ceará (UFC). Publicado em: 2012
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7. Sucrose-Phosphate Synthase from Synechocystis sp. Strain PCC 6803: Identification of the spsA Gene and Characterization of the Enzyme Expressed in Escherichia coli
The first identification and characterization of a prokaryotic gene (spsA) encoding sucrose-phosphate synthase (SPS) is reported for Synechocystis sp. strain PCC 6803, a unicellular non-nitrogen-fixing cyanobacterium. Comparisons of the deduced amino acid sequence and some relevant biochemical properties of the enzyme with those of plant SPSs revealed import
American Society for Microbiology.
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8. Purification and Characterization of an NAD-Malic Enzyme from Bradyrhizobium japonicum A1017
An NAD-malic enzyme was purified to homogeneity from Bradyrhizobium japonicum A1017, and its molecular characteristics were surveyed. The enzyme exhibited native and subunit molecular masses of 388 and 85 kDa, respectively, suggesting that it exists as a homotetramer, and was activated by metabolic intermediates in glycolysis. The role of the enzyme in bacte
American Society for Microbiology.
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9. Glucosinolate Biosynthesis (Further Characterization of the Aldoxime-Forming Microsomal Monooxygenases in Oilseed Rape Leaves).
The initial steps in glucosinolate biosynthesis are thought to proceed from amino acids, via N-hydroxy amino acids, to aldoximes. We showed previously that microsomes from green leaves of oilseed rape (Brassica napus cv Bienvenu) contain two distinct monooxygenases that catalyze the conversion of homophenylalanine and dihomomethionine to their respective ald
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10. The LCB2 gene of Saccharomyces and the related LCB1 gene encode subunits of serine palmitoyltransferase, the initial enzyme in sphingolipid synthesis.
The first and committed step in synthesis of the ceramide moiety of sphingolipids is catalyzed by serine palmitoyltransferase (EC 2.3.1.50), which condenses palmitoyl-CoA and serine to form 3-ketosphinganine. This step is thought to be tightly regulated to control the synthesis of sphingolipids, but data supporting this hypothesis are lacking mainly because
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11. Drosophila topoisomerase I: isolation, purification and characterization.
We have purified and characterized topoisomerase I from Drosophila melanogaster. The molecular weight of the enzyme is 135,000; 100,000, 90,000, and 65,000 molecular weight products result from degradation of the enzyme. The enzyme relaxes both positive and negative supercoiled DNA. Mg++ is not absolutely required, but stimulates the enzymatic activity consi
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12. Partial Purification and Characterization of β-glucosidase fromMonascus sanguineus
The aim of the present work was to study the production and characterization of β-glucosidase from Monascus sanguineus. Agro-waste residues were screened to obtain the maximum yield of enzyme. Jack fruit seed was the best substrate for enzyme production. Studies on the optimization of pH and temperature showed acidic pH favorable for enzymatic activity, whe
Braz. arch. biol. technol.. Publicado em: 14/10/2014