NADPH Oxidases Methods and Protocols
This detailed volume explores the NADPH oxidase family of enzymes in human physiology and genetic disease, in which early discoveries represent prime examples of the finest translational “from bed to bench and back” studies. Methods are included for testi
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Ulla G. Knaus Thomas L. Leto Editors
NADPH Oxidases Methods and Protocols
METHODS
IN
MOLECULAR BIOLOGY
Series Editor John M. Walker School of Life and Medical Sciences University of Hertfordshire Hatfield, Hertfordshire AL10 9AB, UK
For further volumes: http://www.springer.com/series/7651
NADPH Oxidases Methods and Protocols
Edited by
Ulla G. Knaus Conway Institute, School of Medicine, University College Dublin, Dublin, Ireland
Thomas L. Leto Laboratory of Clinical Immunology and Microbiology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, USA
Editors Ulla G. Knaus Conway Institute, School of Medicine University College Dublin Dublin, Ireland
Thomas L. Leto Laboratory of Clinical Immunology and Microbiology National Institute of Allergy and Infectious Diseases, National Institutes of Health Bethesda, MD, USA
ISSN 1064-3745 ISSN 1940-6029 (electronic) Methods in Molecular Biology ISBN 978-1-4939-9423-6 ISBN 978-1-4939-9424-3 (eBook) https://doi.org/10.1007/978-1-4939-9424-3 © Springer Science+Business Media, LLC, part of Springer Nature 2019 This work is subject to copyright. All rights are reserved by the Publisher, whether the whole or part of the material is concerned, specifically the rights of translation, reprinting, reuse of illustrations, recitation, broadcasting, reproduction on microfilms or in any other physical way, and transmission or information storage and retrieval, electronic adaptation, computer software, or by similar or dissimilar methodology now known or hereafter developed. The use of general descriptive names, registered names, trademarks, service marks, etc. in this publication does not imply, even in the absence of a specific statement, that such names are exempt from the relevant protective laws and regulations and therefore free for general use. The publisher, the authors, and the editors are safe to assume that the advice and information in this book are believed to be true and accurate at the date of publication. Neither the publisher nor the authors or the editors give a warranty, express or implied, with respect to the material contained herein or for any errors or omissions that may have been made. The publisher remains neutral with regard to jurisdictional claims in published maps and institutional affiliations. This Humana imprint is published by the registered company Springer Science+Business Media, LLC part of Springer Nature. The registered company address is: 233 Spring Street, New York, NY 10013, U.S.A.
Preface NADPH oxidases are the only enzymes solely dedicated to reduce molecular oxygen to superoxide and, under some circumstances, to hydrogen peroxide (H2O2). NADPH oxidases, also termed NOX or DUOX (in the presence of an additional peroxidase-like extracellular N-terminal domain), are expressed widely in prokaryotes and eukaryotes. The NOX/DUOX family consists of several structurally and functionally related members such as five NOX and two DUOX isoforms in humans. Although the general mechanism of elect
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