Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.11.1.7 (peroxidase)
 65,474 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Until now o-dianisidine was used as an indicator substance in a test system for the determination of diamine oxidase. More recently, however, this substance was also used to measure ceruloplasmin activity. A study of the test principles revealed that o-dianisidine was the one denominator for both enzymes. As it was found for diamine oxidase the indicator was oxidized via peroxidase mediated H2O2 cleavage. Ceruloplasmin, however, oxidized o-dianisidine directly with resulting free radical formation. An addition of histamine dihydrochloride or putrescine dihydrochloride to an incubation mixture, containing ceruloplasmin as enzyme and o-dianisidine or p-phenylene-diamine as substrates, produced an activation of the enzyme, being more than 10-fold in the presence of 1 X 10(-2) M putrescine at pH 7.0. It was assumed that an allosteric effect of the dihydrochloride component might be responsible for this activation. When the activity of purified diamine oxidase was determined by the o-dianisidine test and by the isotope assay, a very good correlation between both methods was found. But, in a mixture of diamine oxidase and ceruloplasmin, no differentiation between the two enzymic activities by the o-dianisidine test was possible. This observation demonstrated an interference of ceruloplasmin when the o-dianisidine method was used for the determination of diamine oxidase activity. To apply our findings also in vivo the amine oxidase activity increasing in guinea-pig plasma during inflammation, was determined by the o-dianisidine test and by specific methods for some amine oxidase. Despite an enhanced oxidation of the o-dianisidine observed, only an increase of ceruloplasmin activity was found. It was concluded that ceruloplasmin had no 'histaminase activity' as has been assumed by other authors using the o-dianisidine test.
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PMID:Determination of histaminase (diamine oxidase) activity by o-dianisidine test: interference of ceruloplasmin. 40 58

Various enzymes in the semen of men were examined to see if any could be related to measures of fertility. Fumarase activity was highly correlated with sperm number and percentage motility. Diamine oxidase activity was higher in samples with sperm counts of less than 20 X 10(6)/ml and aperm motility of less than 20%. Monoamine oxidase, adenine deaminase and prostaglandin dehydrogenase were undetectable in significant amounts in all samples, while peroxidase and adenosine deaminase were not correlated with sperm count and motility. It is suggested that the simple spectrophotometric assays for fumarase and diamine oxidase could form the basis of a routine assessment of human semen samples for estimation of male infertility.
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PMID:The development of a qualitative assay for male infertility from a study of enzymes in human semen. 41 Sep 26

Effect of reoxygenation of the serum enzymatic activities and protein fractions in dog with acute myocardial infarction. The enzymatic activitites creatin phosphokinase (CPK; E.C. 2.7.3.2), glutamate oxalacetate transaminase (GOT; E.C. 2.6.1.1.), diamine oxidase (DAO; E.C. 1.4.3.6.), monoamine oxidase (MAO; E.C. 1.4.3.4.), catalase (E.C. 1.2.1.6.), peroxidase (E.C. 1.2.1.6.) and the protein fractions levels are measured in the dog serum during experimental myocardial infarction, followed by 2 hours of reoxygenation. The alpha, and alpha2 globuline serum proteins increase during anoxic period; after reperfusion alpha1 globuline content further increase again, while alpha2 globuline fraction decrease to control values. The enzymatic activities, particulary CPK, DAO and MAO, significantly enhance during coronary occlusion. After riperfusion the DAO, GOT and peroxidase activities decrease, while the CPK, atalase and MAO activities further increase, particulary at the early stage of the reperfusion. These results are discussed interms of cellular mechanism, induced by oxygen readmission.
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PMID:[Behavior of some serum enzymes and proteins in experimental revascularization of acute myocardial infarct]. 80 32

A specific peroxidase-coupled activity staining method for diamine oxidase (DAO) was developed. Diaminobenzidine was found to inhibit DAO and to give rise to unspecific staining. Among several other reagents 4-Cl-1-naphthol was found to be most suitable. Using specific activity staining DAO could be visualized in polyacrylamide gels as a high-molecular-weight complex, which could be dissociated by Tween 20 but not by NP-40, Triton X-100, or Chaps.
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PMID:A specific peroxidase-coupled activity stain for diamine oxidases. 144 26

Recently four tissue toxic proteins namely major basic protein (MBP), eosinophil peroxidase (EPO), eosinophil-derived neurotoxin (EDN), and eosinophil cationic protein (ECP) were found in eosinophilic leucocytes. Although the characteristics of these proteins concerning tissue damage in the local site of type I allergic reaction have been investigated mainly in lower respiratory tract, the actual clinico-pathological roles of these proteins in nasal allergy are not clarified. Contrary, eosinophils also have histaminase, arylsulfatase, phospholipase D, which are considered to act on a negative feedback mechanism in allergic reaction through inactivation of chemical mediators. Therefore, estimation of ECP and simultaneously arylsulfatase B in nasal secretion and the sera from patients with nasal allergy may clarify the dynamics of clinico-pathological state, especially in the late phase of allergic reaction in each patients. ECP concentrations in the nasal secretions from 22 patients and in the sera from 12 patients with nasal allergy were measured by RIA method. The activities of arylsulfatase B in the nasal secretions and the sera were also estimated in the same specimens as ECP by measuring its hydrolytic activity using p-nitro cathecol sulfate as a substrate. The results obtained were as follows; 1) There was a significant correlation between ECP concentrations in the nasal secretions and the severities of clinical symptoms, especially the degree of nasal obstruction. ECP concentrations also significantly correlated to the score of eosinophilic leucocytes in the nasal smears. 2) The serum ECP concentrations significantly correlated to the number of eosinophilic leucocytes in the peripheral blood, and also showed slight tendency of correlation to the severity of clinical symptoms.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Study on eosinophil cationic protein (ECP) and arylsulfatase B in nasal secretions and sera from patients with nasal allergy]. 188 31

In order to investigate the availability and release of enzymes from eosinophilic granulocytes in response to a variety of stimuli, guinea pig peritoneal eosinophils were obtained after repeated intraperitoneal injections of freeze-dried Trichinella spiralis larvae. The activities of the enzymes peroxidase, arylsulfatase B, beta-glucuronidase, aminopeptidase, histaminase, cytochrome c oxidase, acid phosphatase, adenosine triphosphatase and glucose 6-phosphatase, and the major basic protein (MBP) were studied histochemically and, in part, also biochemically. Eosinophils were incubated with the following substances: histamine, platelet activating factor, calcium ionophore, compound 48/80, leukotriene B4, prostaglandins E1, and E2, heparin, and eosinophil-chemotactic factors from neutrophils and lymphocytes. Eosinophils displayed a selective and stimulus-dependent enzyme and MBP reaction. Calcium ionophore and compound 48/80 provoked a release of cytotoxic major basic protein, partly associated with peroxidase release, while leukotriene B4 and eosinophil chemotactic factors caused histaminase and peroxidase release and activated leucinaminopeptidase. Heparin and calcium ionophore induced release of both MBP and histaminase. These data support the concept that eosinophils exhibit either inflammatory or cytotoxic, or antiinflammatory properties upon stimulation by various agents.
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PMID:Activation and release of enzymes and major basic protein from guinea pig eosinophil granulocytes induced by different inflammatory stimuli and other substances. A histochemical, biochemical, and electron microscopic study. 275 82

In order to study changes in serum histaminolytic enzyme activity in allergic individuals following allergen challenge, serum histaminase activity was measured using the 0-dianisidine peroxidase method in patients with Japanese cedar pollinosis. Significantly higher serum histaminase activity was detected in pollen season than out of season and a significant relationship was recognized between serum histaminase activity and the severity of nasal symptoms.
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PMID:Changes of serum histaminase activity in pollinosis. 309 86

A knowledge of eosinophil granulocytes is indispensable for the study of hypereosinophilia. For this reason, the most recent findings relating to eosinophil morphology, production/regulation mechanism, and function are reported. Particular attention is given to enzyme populations, local control mechanisms and eosinophil cell surface receptors. Among the various enzymes present in the eosinophil, major basic protein (MBP), with its capacity to damage the cells of many organs, plays an important part; other enzymes include eosinophil peroxidase (EPO), arylsulphatase B, phospholipase D, histaminase and cationic proteins (ECP). Factors influencing eosinophil tissue concentrations and mode of action are considered. Recent findings agree on the role of eosinophils in immunological reactions and parasitic infestations: eosinophil plays a part in an immunological physiopathological sequence: it may, act as a killer cell with selective action against invading parasites, or it may be an immune modulator, anti-inflammatory cell able to surround inflammatory reactions and prevent them from spreading.
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PMID:[Hypereosinophilias of the blood. I. Eosinophilic granulocytes]. 392 3

1. The rate of oxidative deamination of 1,5-diaminopentane by pea-seedling extracts, which contain diamine oxidase [diamine-oxygen oxidoreductase (deaminating), EC 1.4.3.6], was increased by adding pyridoxal or pyridoxal phosphate. 2. Evidence was obtained that pyridoxal does not activate the apoenzyme of diamine oxidase, but prevents the inactivation of the enzyme. 3. This inactivation only occurred when 1,5-diaminopentane was the substrate and depended on a second thermolabile factor in the extract besides the diamine oxidase. 4. Purified diamine oxidase, when catalysing the oxidation of 1,5-diaminopentane, was rapidly inactivated in the presence of peroxidase. 5. The inactivation was prevented not only by pyridoxal and pyridoxal phosphate but also by several unrelated compounds including alpha-oxoglutarate, catechol and o-aminobenzaldehyde. 6. It is suggested that peroxidase catalyses the further oxidation of the product of the oxidative deamination of 1,5-diaminopentane to a compound that inactivates diamine oxidase. 7. The results diminish the relevance of previous evidence that plant diamine oxidase contains pyridoxal phosphate.
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PMID:The inactivation of pea-seedling diamine oxidase by peroxidase and 1,5-diaminopentane. 496 23

Because imidazole acetic acid (IAA), a product of histamine catabolism was shown to inhibit histaminase release from human polymorphonuclear leukocytes (PMNs), the effect of this compound on other neutrophil functions was investigated. IAA at concentrations of 10(-10) or more inhibited histaminase release induced by particle-bound C3b, the larger fragment of the activated form of the third component of complement. Release of histaminase induced by aggregated IgG, phorbal myristate acetate (PMA), formyl-methionyl-leucyl-phenylalanine (FMLP) and calcium ionophore was not affected by IAA. In addition IAA had no effect on release of beta-glucuronidase, myeloperoxidase, and lysozyme or on phagocytosis and superoxide generation. IAA did modestly inhibit neutrophil chemotaxis. These findings suggest a highly specific modulating effect of the histamine catabolite IAA on complement-mediated PMN function.
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PMID:Specific modulation of complement-dependent human granulocyte function by imidazole acetic acid. 625 58


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