5,399 research outputs found

    Renalase, a catecholamine-metabolising enzyme?

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    Recently, a new FAD-dependent amine oxidase, renalase, was described. It was secreted by the kidney into the blood and shown to have significant cardiovascular actions, which were attributed to its catecholamine-metabolising activity. The authors concluded that renalase might be an important regulatory factor in human (patho)physiology. The catecholamine-metabolising activity of renalase in plasma contrasts with previous investigations where catecholamines were found to be stable in human plasma, provided autoxidation is prevented by an antioxidant. The claim of catecholamine-metabolising activity of renalase was based on the generation of H2O2 during incubation of the enzyme with catecholamines. Careful inspection and calculations of the data lead to the conclusion that the rate of H2O2 generation is far too low to be ascribed to enzymatic conversion of catecholamines by renalase. Renalase may well have important cardiovascular functions, but there is no proof that its actions are mediated through catecholamine-metabolising activity

    ExplorEnz: the primary source of the IUBMB enzyme list

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    ExplorEnz is the MySQL database that is used for the curation and dissemination of the International Union of Biochemistry and Molecular Biology (IUBMB) Enzyme Nomenclature. A simple web-based query interface is provided, along with an advanced search engine for more complex Boolean queries. The WWW front-end is accessible at http://www.enzyme-database.org, from where downloads of the database as SQL and XML are also available. An associated form-based curatorial application has been developed to facilitate the curation of enzyme data as well as the internal and public review processes that occur before an enzyme entry is made official. Suggestions for new enzyme entries, or modifications to existing ones, can be made using the forms provided at http://www.enzyme-database.org/forms.php

    Charge asymmetry in hadroproduction of heavy quarks

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    A sizeable difference in the differential production cross section of top and antitop quarks, respectively, is predicted for hadronically produced heavy quarks. It is of order αs\alpha_s and arises from the interference between charge odd and even amplitudes respectively. For the TEVATRON it amounts to approximately 5-10% in the region where the cross section is large and could therefore be measured in the next round of experiments. At the LHC the asymmetry can be studied by selecting appropriately chosen kinematical regions.Comment: LaTeX, 5pp, 5 figures, uses revtex. The complete paper, including figures, is also available via anonymous ftp at ftp://ttpux2.physik.uni-karlsruhe.de/ , or via www at http://www-ttp.physik.uni-karlsruhe.de/cgi-bin/preprints/ Final version as published in Phys.Rev.Let
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