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Enzyme immunoassays have developed into a powerful assay technology, transcending several discipline boundaries, extensively applied as a tool in fields other than enzymology and immunology. This volume reflects the rapid progress in the applications of this technique, providing a basic understanding of these techniques and a practical guideline for the choice and experimental detail.

Immunoenzyme technique. --- Science. --- Chemistry. --- Natural history. --- Immunoenzyme Techniques --- Immunoenzyme Techniques. --- 577.15.083.3 --- Antibody Enzyme Technic, Unlabeled --- Enzyme-Labeled Antibody Technic --- Immunoenzyme Technics --- Immunoperoxidase Technics --- Peroxidase-Antiperoxidase Complex Technic --- Peroxidase-Labeled Antibody Technic --- Antibody Enzyme Technique, Unlabeled --- Enzyme Immunoassay --- Enzyme-Labeled Antibody Technique --- Immunoassay, Enzyme --- Immunoperoxidase Techniques --- Peroxidase-Antiperoxidase Complex Technique --- Peroxidase-Labeled Antibody Technique --- Antibody Technic, Enzyme-Labeled --- Antibody Technic, Peroxidase-Labeled --- Antibody Technics, Enzyme-Labeled --- Antibody Technics, Peroxidase-Labeled --- Antibody Technique, Enzyme-Labeled --- Antibody Technique, Peroxidase-Labeled --- Antibody Techniques, Enzyme-Labeled --- Antibody Techniques, Peroxidase-Labeled --- Enzyme Immunoassays --- Enzyme Labeled Antibody Technic --- Enzyme Labeled Antibody Technique --- Enzyme-Labeled Antibody Technics --- Enzyme-Labeled Antibody Techniques --- Immunoassays, Enzyme --- Immunoenzyme Technic --- Immunoenzyme Technique --- Immunoperoxidase Technic --- Immunoperoxidase Technique --- Peroxidase Antiperoxidase Complex Technic --- Peroxidase Antiperoxidase Complex Technique --- Peroxidase Labeled Antibody Technic --- Peroxidase Labeled Antibody Technique --- Peroxidase-Antiperoxidase Complex Technics --- Peroxidase-Antiperoxidase Complex Techniques --- Peroxidase-Labeled Antibody Technics --- Peroxidase-Labeled Antibody Techniques --- Technic, Enzyme-Labeled Antibody --- Technic, Immunoenzyme --- Technic, Immunoperoxidase --- Technic, Peroxidase-Antiperoxidase Complex --- Technic, Peroxidase-Labeled Antibody --- Technics, Enzyme-Labeled Antibody --- Technics, Immunoenzyme --- Technics, Immunoperoxidase --- Technics, Peroxidase-Antiperoxidase Complex --- Technics, Peroxidase-Labeled Antibody --- Technique, Enzyme-Labeled Antibody --- Technique, Immunoenzyme --- Technique, Immunoperoxidase --- Technique, Peroxidase-Antiperoxidase Complex --- Technique, Peroxidase-Labeled Antibody --- Techniques, Enzyme-Labeled Antibody --- Techniques, Immunoenzyme --- Techniques, Immunoperoxidase --- Techniques, Peroxidase-Antiperoxidase Complex --- Techniques, Peroxidase-Labeled Antibody --- Enzymes. Catalysts of biological reactions. Enzymology--?.083.3 --- 577.15.083.3 Enzymes. Catalysts of biological reactions. Enzymology--?.083.3 --- Cytochemistry. --- Cell chemistry --- Biochemistry --- Cytology --- Antibody enzyme techniques, Unlabeled --- Immunoperoxidase technique --- Peroxidase labeled antibody technique --- Enzymatic analysis --- Immunoassay --- Immunology --- Protein binding --- Technique --- Basic Sciences. Chemistry --- Biochemistry. --- Enzymimmunassay. --- Enzym immunoassay. --- Immunoenzyme Techniques - laboratory manuals --- Enzymes --- Immunochemical analysis

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The peroxiredoxin family was discovered approximately 30 years ago and is now recognized as one of the most important families of enzymes related to antioxidant defense and cellular signaling. Peroxiredoxin 6 shares the basic enzymatic functions that characterize this family, but also exhibits several unique and crucial activities. These include the ability to reduce phospholipid hydroperoxides, phospholipase A2 activity, and an acyl transferase activity that is important in phospholipid remodeling. This book describes the available models for investigating the unique functions of PRDX6 and its role in normal physiological function, as well its roles in the pathophysiology of diseases including cancer, diseases of the eye, and male fertility.

n/a --- NADPH (nicotinamide adenine dinucleotide phosphate) oxidase --- sperm capacitation --- phospholipid hydroperoxide --- cornea --- peroxidase --- phospholipase A2 --- 1-Cys Prdx --- knock-in mouse --- drug delivery --- antioxidant activity --- sulfinic acid --- radioprotection --- spermatozoa --- peroxiredoxin 6 --- mass spectroscopic analysis --- knockout mouse --- phospholipase A2 activity --- liposomes --- mitochondrial membrane potential --- lipid peroxidation --- PLA2 activity --- ionizing radiation --- glutathione peroxidase --- Peroxiredoxin --- Prdx6 structure --- membrane repair --- substrate binding --- inflammation --- reactive oxygen species --- Prdx6 --- sulfonic/sulfinic acid --- Fuchs’ endothelial corneal dystrophy --- endothelium --- fertilization --- peroxidatic cysteine --- thioredoxin fold --- redox balance --- surfactant protein A --- diabetes --- oxidative stress --- Fuchs' endothelial corneal dystrophy

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This reprint is focused on recent novel research related to the role of plant cell walls under biotic and abiotic stresses, which was published in the Special Issue “Plant Cell Wall Plasticity under Stress Situations” of the Plants journal. Considering the importance of this plant cell structure in a plethora of plant development processes, this book focused on unraveling the roles of different cell wall components and their turnover in plant defense against pathogens and adaptative responses, in cell wall hydration ability, and in the development of primitive water transport systems in non-vascular plants.

Research & information: general --- Biology, life sciences --- plant cell wall composition --- expansins --- water stress --- salt stress --- Physcomitrella --- hydroxycinnamyl alcohols --- plant evolution --- peroxidase --- abiotic stress --- bean --- Pseudomonas --- cell wall --- plant defense --- disease resistance --- 2,6-dichloroisonicotinic acid --- INA --- pectin --- calcium --- boron --- homogalacturonan --- rhamnogalacturonan II --- Botrytis cinerea --- Colletotrichum higginsianum --- dehydration --- Allium and X-ray microscopy --- β-glucanases --- β-glucans --- cell wall polysaccharides --- plant development --- environmental stress --- n/a

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Biocatalysis, the application of enzymes as catalysts for chemical synthesis, has become an increasingly valuable tool for the synthetic chemist. Enzymatic transformations carried out by enzymes or whole-cell catalysts are used for the production of a wide variety of compounds ranging from bulk to fine chemicals. The primary consideration for the incorporation of biotransformation in a synthetic sequence is regio- and stereocontrol that can be achieved with enzyme-catalyzed reactions. Biotransformations are thus becoming accepted as a method for generating optically pure compounds as well as for developing efficient routes to target compounds. This Special Issue aims to address the main applications of biocatalysts, isolated enzymes, and whole microorganisms in the synthesis of bioactive compounds and their precursors.

8-hydroxydaidzein --- stable --- soluble --- anti-inflammation --- amylosucrase --- Deinococcus geothermalis --- coumarin --- biotransformation --- filamentous fungi --- selective hydroxylation --- bromination --- chlorination --- pharmaceuticals --- active agent synthesis --- biocatalysis --- haloperoxidase --- halogenase --- glycosyltransferase --- Glycine max (L.) Merr. --- HPLC/MS --- isoflavone aglycone-rich extract --- isoflavone α-glucoside --- alkene cleavage --- aryl alkenes --- basidiomycota --- carotene degradation --- dye-decolorizing peroxidase (DyP) --- manganese --- Komagataella pfaffii --- Pleurotus sapidus --- monoterpenes --- limonene --- glycerol --- mevalonate pathway --- reaction engineering --- bioprocess --- biocatalyst --- two-liquid phase fermentation --- in situ product removal --- lipase --- unsaturated fatty acid --- oxidative cleavage --- oxidation --- adaptation --- UV/NTG mutagenesis --- psychrotrophs --- terpenes

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This Special Issue aims to highlight the dual potential of novel biocatalytic processes, where the first part is dedicated to waste valorization for the production of high value products, while the second part is focused on the detoxification of pollutants. Several examples of microbial systems employed for the valorization of waste streams derived by the forest, agricultural, and food industries or the use of whole-cell or enzyme approaches for the removal of nitrogen or dyes from industrial wastewaters are provided. Last but not least, an example of the utilization of polyhydroxyalkanoates (PHAs) was highlighted for the production of fatty acids, which were used for the enzymatic synthesis of sugar esters with antimicrobial properties.

mixotrophic --- heterotrophic --- lipids --- fatty acid methyl esters --- dairy wastewater --- birch hydrolysate --- green algae --- Coelastrella --- Chlorella --- DyP peroxidase --- oxidoreductase --- reactive dye --- decolorization --- biopolymers --- medium chain length polyhydroxyalkanoates (PHA) --- hydrolysed waste cooking oil --- Pseudomonas putida KT2440 --- biocatalysis --- bioprocess --- polyhydroxyalkanoate --- (R)-3-hydroxyacids --- sugar esters --- antimicrobial --- anammox --- immobilization --- wastewater treatment --- polyvinyl alcohol --- olive mill waste --- lignocellulosic residues --- Ganoderma lucidum --- Pleurotus ostreatus --- medicinal mushrooms --- glucan --- prebiotic --- Lactobacillus --- Bifidobacterium --- waste valorization --- laccase --- genome-mining --- heterologous expression --- Pseudomonas --- non-digestible oligosaccharides --- Celluclast® --- cellobiose --- conduritol-B-epoxide --- lignocellulose enzyme hydrolysis --- n/a