Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.11.1.7 (peroxidase)
65,474 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The mannosephilic haemagglutinins of Pseudomonas aeruginosa were found to agglutinate cells of Escherichia coli O128B12, to be adsorbed onto them and to attach peroxidase to them. These reactions were specifically inhibited by D-mannose. No agglutination by this Pseudomonas haemagglutinin was obtained when several other enteropathogenic types of Escherichia coli and some other Gram-negative bacteria were examined. Concanavalin A, which also reacted with Escherichia coli O128B12 cells, interacted with some of the other bacteria examined, too. Escherichia coli O128B12 was not agglutinated by the Pseudomonas galactosephilic haemagglutinins and those of the plant Phaseolus vulgaris. Its maximal agglutination by the Pseudomonas mannosephilic haemagglutinins was obtained employing cells grown for 4-6 h in conventional media. The growth temperature, aeration and presence of certain amino acids, but not D-mannose, in the culture medium had some effect on the agglutination in tensity; pH 6-8 was optimal for it and only at pH 3.0-3.2 no agglutination was observed. Treatment of the bacteria by proteolytic enzymes, ethanol or formaldehyde did not alter their agglutinability by either the Pseudomonas lectin or by antibodies produced against them in rabbits. Heating of the bacteria to 100 degrees C prevented their agglutination by the Pseudomonas lectin and lowered their ability to adsorb it, but did not significantly affect their reactions with the rabbit antibodies.
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PMID:Specific agglutination of Escherichia coli O128B12 by the mannose-binding proteins of Pseudomonas aeruginosa. 2 70

Staining of glutaraldehyde-fixed mammalian cells with peroxidatic enzymes (horseradish peroxidase or horse heart cytochrome c) greatly enhances resolution of their structure under phase microscopy. The topography of cell processes and regions of intercellular contact and overlapping is resolved precisely, even in dense cultures mounted in media which ordinarily do not permit clear demonstration of these areas. The technique is therefore a useful aid to the study of cultured cells with phase optics. Labeling depends on introducing free aldehydes into cells through the use of bifunctional fixatives such as glutaraldehyde. Acetone or formaldehyde fixation prevents staining, and labeling intensity is greatly diminished by pretreatment with spermine, a polyamine that reacts with glutaraldehyde. Electron microscopy reveals that peroxidase tags membranes preferentially; some areas are labeled smoothly, others in a punctate manner. Ribosomes are sharply contrasted, but nuclei remain unstained. Cytochrome c labels condensed nuclear chromatin intensely, and also stains ribosomes and portions of the cytoplasmic ground substance; membranes are mostly unmarked.
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PMID:Use of peroxidatic-enzyme staining to enhance resolution of cultured mammalian cells under phase microscopy. 4 31

Endogenous mannary gland peroxidase in acinar cells of prelactating and lactating rats is revealed in tannic acid-formaldehyde-glutaraldehyde-fixed tissue by means of the standard diaminobenzidine procedure. Diaminobenzidine cytochemical reaction product is present in perinuclear cisternae, in the granular endoplasmic reticulum and in Golgi apparatus of functionally differentiated secretory cells. The mammary gland peroxidase is thought to represent lactoperoxidase. Peroxidase staining is diminished or absent in acinar cells of hypophysectomized and ovariectomized rats, in normal rats during early pregnancy and in nonpregnant mature females. Endogenous peroxidase or a heme protein with peroxidatic activity may be considered an ultracytochemical marker enzyme for acinar cells actively engaged in lactogenesis.
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PMID:Ultrastructural localization of endogenous mammary gland peroxidase during lactogenesis in the rat results after tannic acid-formaldehyde-glutaraldehyde fixation. 4 72

The variability of results to demonstrate the peroxidase of platelets has been attributed to an inhibition of the enzyme by glutaraldehyde. In order to eliminate this difficulty, two new methods have been employed prior to incubation in the diaminobenzidine medium: 1. Fixation was omitted. 2. Fixation was performed in a mixture of tannic acid-formaldehyde glutaraldehyde. With these two procedures, intense and reproducible peroxidase staining of human platelets and chicken thrombocytes was obtained. Only when the fixation procedure was omitted could the peroxidase of rat platelets be demonstrated histochemically. The importance of the detection the peroxidase as a marker enzyme of the megakaryocyte cell line and the relationships of this peroxidase with those of leukocyte peroxidases are discussed.
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PMID:[Improved methods for the cytochemical demonstration of platelet peroxidase (author's transl)]. 6 67

Motilin-immunoreactive cells in the human and monkey duodenum and upper jejunum were investigated by immunofluorescence (IF) and peroxidase-antiperoxidase (PAP) techniques using antibodies against synthetic 13-norleucine motilin and synthetic porcine motilin. Contrary to previous reports, we have demonstrated that motilin-immunoreactive cells are a distinct cell population that does not correspond to 5-hydroxytryptamine-containing enterochromaffin (EC-) cells. EC-cells, indentified by formaldehyde-induced fluorescence (FIF) or by argentaffinity (AA), do not react with either antisera. EC-cells of the monkey, utilizing one method (PAP), reacted to one antiserum very weakly. This reaction was also suppressed by absorption with 13-norleucine motilin. It is suggested that the EC-cells of the monkey contain either a very small amount of motilin or another peptide that exhibits a part of the amino acid sequence of motilin. The discrepancy between these results and those of other authors can be explained by the different reactivity of the antisera used.
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PMID:Immunohistochemical localization of motilin in endocrine non-enterochromaffin cells of the small intestine of humans and monkey. 10 74

The marine bacteria Beneckea harveyi and Photobacterium leiognathi were shown to bear mannose-containing binding sites for the mannosephilic lectins of Pseudomonas aeruginosa and concanavalin A (Con A). The interaction between the lectins and the marine bacteria was demonstrated by the bacteriagglutination test, by adsorption of the lectins onto the bacteria and by mannose-specific peroxidase-binding to the lectin-coated bacteria. Treatment of the bacteria with formaldehyde, phenol, ethanol or boiling them for 15 min, did not alter their ability to adsorb the lectins. The growth rate of the marine bacteria was unaffected when either the Pseudomonas lectins or Con A was added to the culture medium.
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PMID:Interaction of the mannosephilic lectins of Pseudomonas aeruginosa with luminous species of marine enterobacteria. 12 Sep 27

Two different fixatives were applied to human gastric mucosa for the study of antigenic marker substances. The first consists of 96% ethanol and 1% acetic acid (EA method), the second of 4% formaldehyde, 0.5% picric acid and 0.25% glutaraldehyde (FPG method). Samples of resected gastric specimens were fixed, dehydrated and cleared in benzene and embedded in paraplast. The morphology of gastric tissue was well preserved by both methods and permitted the simultaneous application of classical staining procedures and the immunoenzyme peroxidase technique for the demonstration of antigenic substances. The following marker substances could be demonstrated: Pepsinogen I and II group, surface epithelial antigen, parietal cell antigen, chief cell antigen, antral mucous cell antigen, carcinoembryonic antigen, goblet cell antigen and common site antigen of leucocytes. Various factors responsible for nonspecific reactions, such as endogeneous peroxidase activity and protein interactions were studied. The latter were circumvented by the use of highly purified antibodies or immunoglobulin fractions. The EA method proved to be the method of choice for future routine application of combined classical histology and immunoenzyme histology in gastric and intestinal diseases.
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PMID:Immunohistochemical studies on human gastric mucosa. Procedures for routine demonstration of gastric proteins by immunoenzyme techniques. 15 Jan 10

Multispecific antigen-binding fragments (Fab) from rabbit antisera against rat very low density lipoproteins (VLDL) and Fab against rat low density lipoproteins that were monospecific for the B apoprotein were conjugated to horseradish peroxidase. Conjugates were incubated with 6-mum frozen sections from fresh and perfusion-fixed livers and with tissue chopper sections (40 mum thick) from perfusion-fixed livers. In the light microscope, specific reaction product was present in all hepatocytes of experimental sections as intense brown to black spots whose locations corresponded to the distribution of the Golgi apparatus: along the bile canaliculi, near the nuclei, and between the nuclei and bile canaliculi. Perfusion fixation with formaldehyde produced satisfactory ultrastructural preservation with retention of lipoprotein antigenic determinants. In the electron microscope, patches of cisternae and ribosomes of the rough endoplasmic reticulum (ER) and particularly its smooth-surfaced ends, vesicles located between the rough ER and the Golgi apparatus, the Golgi apparatus and its secretory vesicles and VLDL particles in the space of Disse all bore reaction product. The tubules and vesicles of typical hepatocyte smooth ER did not contain reaction product, nor did the osmiophilic particles contained therin. The localization obtained in this study together with other evidence suggests a sequence for the biosynthesis of VLDL that differs in some respects from that proposed by others: (a) the triglyceride-rich particle originates in smooth ER where triglycerides are synthesized; (b) at the junction of the smooth and rough ER the particle receives apoproteins synthesized in the rough ER; (c) specialized tubules transport the particle, now a nascent lipoprotein, to the Golgi apparatus where concentration occurs in secretory vesicles; (d) secretory vesicles move to the sinusoidal surface where the particles are secreted into the space of Disse by fusion of the vesicular membrane with the plasma membrane of the hepatocyte.
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PMID:Subcellular localization of B apoprotein of plasma lipoproteins in rat liver. 17 30

5-Hydroxytryptamine (serotonin)-containing neurons in the rat's medullary raphe and interfascicularis hypoglossi cell groups were identified by means of autoradiography following prolonged intraventricular administration of 5-hydroxy[(3)H]tryptamine, fluorescence histochemistry for the demonstration of endogenous 5-hydroxytryptamine, and microspectrofluorimetric analysis of excitation and emission spectra. Immunocytochemical methods (the unlabeled primary antibody-peroxidase antiperoxidase and indirect immunofluorescence methods) were applied with antisera to substance P in order to localize immunoreactivity in these medullary neurons. It was demonstrated that the raphe nuclei and the interfascicularis hypoglossi nucleus are heterogeneous cell groups that contain: (i) Neurons that display both an uptake-storage capacity for 5-hydroxy[(3)H]tryptamine and a formaldehyde-induced fluorescence with spectral characteristics identical to those of the 5-hydroxytryptamine fluorophor. These cells exhibit high to low fluorescence intensities without detectable substance P-like immunoreactivity. (ii) Neurons with various 5-hydroxytryptamine fluorescence intensities and intense to low degrees of substance P-like immunoreactivity. (iii) Neurons with various degrees of substance P-like immunoreactivity without detectable 5-hydroxytryptamine fluorescence or 5-hydroxy[(3)H]tryptamine uptake and storage capacity. These results indicate that some neurons contain high or low levels of only 5-hydroxytryptamine or substance P, whereas other neurons contain both 5-hydroxytryptamine and substance P in various proportions. The present findings demonstrate the presence of two putative transmitters, a biogenic amine and a polypeptide, within the same neuron in the mammalian central nervous system.
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PMID:Serotonin and substance P coexist i, neurons of the rat's central nervous system. 27 44

gamma-Aminobutyric acid transaminase (GABA-Tase; 4-aminobutyrate:2-oxaglutarate aminotransferase, EC 2.6.1.19) immunoreactivity in the rat's cerebellum was studied by light and electron microscopy with indirect immunofluorescence and peroxidase-antiperoxidase methods. Evidence is presented for neuronal and neuroglial compartments of GABA-Tase. Labeled neurons included stellate, basket, Purkinje, and Golgi cells of the cortex and a few large neurons in the deep nuclei. Labeled neuroglia included those surrounding Purkinje cells, their radial fibers in the molecular layer, and astrocytes in the granular layer and deep nuclei. No evidence for sagittal microzonation was found. At the ultrastructural level, GABA-Tase immunoreactive sites were localized to cell surface membranes, intracellular organelles, and the cytoplasmic matrix. GABA-Tase immunoreactivity at synapses could be localized precisely to pre- and postsynaptic membranes in gamma-aminobutyric acid (GABA)-containing as well as non-GABA-containing neurons. Specific label was absent from tissues treated with normal rabbit preimmune sera. GABA-Tase labeling was more intense in tissues from animals anesthetized with ether than with barbiturates and after formaldehyde fixation without glutaraldehyde. Increased GABA-Tase immunoreactivity was observed on treatment with colchicine, GABA with oxamic acid, GABA, harmaline, norepinephrine and glutamate, or diazepam (in order of decreasing effectiveness). Serotonin produced no detectable change, and apomorphine and muscimol decreased the immunoreactivity.
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PMID:Immunocytochemical localization of gamma-aminobutyric acid transaminase at cellular and ultrastructural levels. 28 44


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