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OverviewThis book offers deep insights into the thermodynamics and molecular structures of the twelve catalytically active isoforms of human carbonic anhydrase (CA) with a particular focus on inhibitor binding for drug design. X-ray crystallographic structures in combination with enzyme kinetic testing provide information on the interaction of CAs and their inhibitors, knowledge which is crucial for rational drug design. CAs are zinc carrying enzymes that catalyse the reversible interconversion of carbon dioxide and bicarbonate and are involved in numerous cellular processes. They are therefore a common target for drugs. The suppression of CA activities through inhibitory compounds has found application for example in diuretics and in glaucoma therapy. In this book methods used to determine binding thermodynamics of inhibitory compounds (Isothermal titration calorimetry, Fluorescent thermal shift assay/differential scanning fluorimetry and others) will be compared in detail. Also typesand chemical synthesis of CA inhibitors, the use of antibodies against CAs as well as inhibitor application in animals are discussed. Full Product DetailsAuthor: Daumantas MatulisPublisher: Springer Nature Switzerland AG Imprint: Springer Nature Switzerland AG Edition: 1st ed. 2019 Weight: 0.895kg ISBN: 9783030127787ISBN 10: 3030127788 Pages: 353 Publication Date: 03 June 2019 Audience: Professional and scholarly , Professional & Vocational Format: Hardback Publisher's Status: Active Availability: Manufactured on demand We will order this item for you from a manufactured on demand supplier. Table of ContentsReviewsAuthor InformationProf. Dr. Daumantas Matulis Vilnius University Life Sciences Center Institute of Biotechnology Department of Biothermodynamics and Drug Design Sauletekio 7, 10257 Vilnius Lithuania Tab Content 6Author Website:Countries AvailableAll regions |