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At least 1,423 records · Page 79Linked to original sources
PubMed1988

Plant hormone interaction and phenolic metabolism in the regulation of russet spotting in iceberg lettuce.

Russet spotting (RS) is a physiological disorder induced in iceberg lettuce (Lactuca sativa L.) by exposure to parts per million levels of ethylene at 5 +/- 2 degrees C. Ethylene induced phenylalanine ammonia-lyase and ionically bound peroxidase activities that correlated with development of RS symptoms. The ethylene-treated tissue had significantly higher lignin content than air control tissue with lignification localized in walls of RS-affected cells. Ethylene also caused the accumulation of the flavonoids (+)catechin and (-)epicatechin and the chlorogenic acid derivatives 3-caffeoyl-quinic acid, 3,5-dicaffeoylquinic acid, and 4,5-dicaffeoylquinic acid. These soluble phenolic compounds were readily oxidized to brown substances by polyphenol oxidase isolated from RS tissue. Ethylene substantially increased ionically bound indole-3-acetic acid (IAA) oxidase activity, while IAA application greatly reduced ethylene-induced phenylalanine ammonia-lyase, peroxidase, and IAA oxidase activities, soluble phenolic content, and RS development.

Journal Article↗
PubMed1977

Properties of enzymes immobilized by the diazotized m-diaminobenzene method.

Some properties of a number of enzymes immobilized by the diazotized m-diaminobenzene (dDAB) method are described. The pH-activity profiles of beta-D-glucosidase, glucoamylase, peroxidase, uricase, and D-glucose oxidase were virtually unchanged on immobilization while those of catalase and dextranase were significantly altered. beta-D-Glucosidase, glucoamylase, and glucose oxidase were found to be more susceptible to denaturation on lyophilization when immobilized than in the native state; however, sorbitol had a marked protective effect in every case examined. Sorbitol was also found to exert a stabilizing effect when lyophilized immobilized preparations were stored. Immobilization marginally improved the stabilities of a number of enzymes to heating at 60 degrees at pH 8.0. The usefulness for continuous reaction of a column of glucoamylase attached to celite was established. The reuse of the solid supports was demonstrated.

Aniline Compounds↗
PubMed1984

Enzyme-histochemical characterization of macrophages in the rat thymus, with special reference to metallophilic cells of the corticomedullary zone.

The cortex and medulla of the normal rat thymus are populated with scattered cells which are strongly positive for acid phosphatase and only weakly (cortex) or moderately (medulla) positive for nonspecific esterase. Corticomedullary zone is characterized, as a specific entity within the thymic tissue, by the presence of very large macrophages, highly positive for acid phosphatase and nonspecific esterase. Moreover, these cells, located exclusively in the corticomedullary zone, show very strong succinic dehydrogenase activity and contain the intracytoplasmic granules of varying size, which are aldehyde fuchsin, PAS, and oil red O positive. The presence of cholesterol was demonstrated within the lipid content.

Acid Phosphatase↗
PubMed2006

Rapid and efficient enzyme encapsulation in a dendrimer silica nanocomposite.

We report the entrapment of horseradish peroxidase and quantitative encapsulation of glucose oxidase within silica nanoparticles by utilizing an amine-terminated dendritic template. Our improved strategy employs a water-soluble biomimetic template which is able to catalyze the condensation of Si(OH)(4) to silica nanoparticles while trapping an enzyme inside the mesoporous material. Kinetic analysis shows enzyme functionality to be mostly unchanged. Also, the role of pI and ionic strength within the encapsulation environment was found to strongly influence encapsulation. These results suggest that the electrostatic manipulation of a strong supramolecular silica-precipitating complex of enzyme and dendrimer has the potential of adding a vast array of chemical and biological activity to hybrid materials. [image: see text] Enzyme immobilization within a silica nanocomposite.

Biocompatible Materials↗
PubMed1992

Bovine neutrophils recruited by endotoxin to a teat cistern continuously produce oxygen radicals and show increased phagocytosis and extracellular chemiluminescence.

Bovine neutrophils were harvested from a teat cistern following endotoxin infusion and were compared with blood neutrophils by measurements of chemiluminescent and phagocytic activity towards C3- and IgG-opsonized and unopsonized yeast particles. Both phagocytosis and luminol-dependent chemiluminescence elicited by all three particles were enhanced in the teat cells. The increase in the luminol-dependent chemiluminescence towards C3- and IgG-opsonized particles was due to an enhanced extracellular release of myeloperoxidase. The observed increase in phagocytosis of unopsonized yeast was shown to reflect the interaction between up-regulated CR3 receptors on the surface of the teat neutrophils and the yeast particles. A high chemiluminescent activity of the teat neutrophils in both the luminol- and lucigenin-dependent systems in the absence of a phagocytic prey indicated that the NADPH oxidase was permanently active and that myeloperoxidase was continuously released by the cells. Treatment of neutrophils with cytochalasin B showed that the chemiluminescence and phagocytosis of teat neutrophils were less sensitive to this drug than that of blood neutrophils. These results indicate that the teat neutrophils have up-regulated their receptors for IgG- and C3-opsonized and unopsonized yeast on the cell surface by the action of actin. The cells also have a permanently active NADPH oxidase dependent on the association with actin and show a higher tendency than blood neutrophils to secrete the content of their primary granules during phagocytosis.

Actins↗
PubMed1993

Antioxidant protection against oxidant-induced damage in cultured gastric mucosal cells.

Gastric epithelium is exposed not only to oxidants generated within the lumen, but also to those produced by ischemia/reperfusion. This study examined the mechanism(s) of oxidant-induced injury to cultured rat gastric mucosal cells, and characterized the antioxidant profile of these cells. Hydrogen peroxide (H2O2), generated by glucose oxidase, damaged cells dose-dependently, as assessed by increased leakage of labeled 51Cr. Glucose oxidase-induced damage was prevented by exogenous catalase (but not by exogenous superoxide dismutase). Chelation of cellular iron with desferrioxamine or phenanthroline specifically protected cells against H2O2, whereas binding of extracellular iron with apotransferrin failed to. Disruption of the glutathione redox cycle at three independent sites rendered cells less resistant to H2O2, whereas inhibition of cellular catalase did not result in sensitization of cells to H2O2. In conclusion, (1) oxidant injury induced by extracellular H2O2 is mediated by intracellular iron; (2) extracellular superoxide is not involved in the damaging process; and (3) the glutathione redox cycle plays a principal role in detoxifying H2O2 as a cellular antioxidant in cultured gastric mucosal cells.

Animals↗
PubMed2005

Study on peptide hydrolysis by aminopeptidases from Streptomyces griseus, Streptomyces septatus and Aeromonas proteolytica.

We developed a spectrophotometric assay for peptide hydrolysis by aminopeptidases (APs). The assay enables the measurement of free amino acids liberated by AP-catalyzed peptide hydrolysis using 4-aminoantipyrine, phenol, peroxidase, and L-amino acid oxidase. We investigated the specificity of bacterial APs [enzymes from Streptomyces griseus (SGAP), Streptomyces septatus (SSAP), and Aeromonas proteolytica (AAP)] toward peptide substrates using this assay method. Although these enzymes most efficiently cleave leucyl derivatives among 20 aminoacyl derivatives, in peptide hydrolysis, the catalytic efficiencies of Phe-Phe hydrolysis by SGAP and SSAP exceed that of Leu-Phe hydrolysis. Furthermore, all enzymes showed the maximum catalytic efficiencies for Phe-Phe-Phe hydrolysis. These results indicate that the hydrolytic activities of bacterial APs are affected by the nature of the penultimate residue or flanking moiety and the length of the peptide substrate.

Aeromonas↗