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020 _a9783030338534
024 7 _a10.1007/978-3-030-33853-4
_2doi
040 _aES-MaUEC
_bspa
_cES-MaUEC
_dES-MaUEC
050 4 _aQH603.M5
_b2019 EB
100 1 _aVekshin, Nikolai
_eautor
_9672501
245 1 0 _aBiophysics of Mitochondria
_cby Nikolai Vekshin.
250 _aFirst edition
264 1 _aCham, Switzerland
_bSpringer International Publishing
_c2019
300 _a1 recurso en línea (XII, 197 páginas)
_b118 ilustraciones
_bonline resource.
336 _2rdacontent
_aTexto
_btxt
337 _2rdamedia
_aelectrónico
_bc
338 _2rdacarrier
_arecurso electrónico
_bcr
347 _atext file
_bPDF
490 0 _aBiomedical and Life Sciences (Springer-11642)
505 0 _aThe mitochondria in the cell -- Early studies -- Structural features -- Are there giant mitochondria and reticulum -- Evolutionary origins -- Reproduction of mitochondria in cell -- Mitochondrial DNA -- Membrane and matrix proteins -- Bioenergetics -- The respiratory chain -- NADH-dehydrogenase -- Succinate dehydrogenase -- Cytochrome oxidase -- Interactions in enzyme-substrate complexes -- Mechanisms of electron transfer -- Membrane synthesis of ATP -- Proton transport and the chemiosmotic hypothesis -- On the measurement of transmembrane potential -- The conformational hypothesis -- Thermal coupling model -- Photo-respiration and photo-induced synthesis of ATP -- Surface photodesorption -- Flavin and ubiquinone of NADH-dehydrogenases are not involved in the transfer of electrons to artificial acceptors -- The lag-period and the pseudo-oscillations in redox-reactions of NADH with DHPIP -- Electron-conformational properties of the flavoprotein fragment of NADH-dehydrogenase -- Resonant energy transfer from mitochondrial proteins to NADH -- Flavin loss from NADH-dehydrogenase complex -- Stabilization of NADH-dehydrogenase by adenosine phosphates -- Dehydrogenase mitochondrial activity in the touch, determined by the decrease in tryptophan fluorescence by formosan -- Rotenone-insensitive NADH oxidation by respiratory chain fragments -- Cytochrome-C shunts oxidation of NADH -- NADH-oxidasation mitochondrial activity in hypotension when you block the respiratory chain -- Do mitochondria swell much? -- Some properties of protomitochondria -- Protomitochondria in liver cells -- Germinal protomitochondria -- Fluorimetric comparison of protomitochondria and mitochondria -- Photometry and fluorimetry of protomitochondria from liver of young and adult rats.-Degradation of mitochondria to lipofuscin during heating and lighting -- Production of superoxide and lipofuscin after the loss of flavin by NADH-dehydrogenase -- Some properties of mitochondrial lipofuscin.
520 3 _aIn this monograph, the author -Head researcher at the Institute of Cell Biophysics of Russian Academy of Sciences- discusses the results of his own long-term studies of mitochondria as well as alternative points of view and experiments of other important researchers in the field. The monograph contains the main aspects of mitochondrial research by a number of physical methods: fluorescence spectroscopy, UV-vis spectrophotometry, IR spectroscopy, light-scattering, optical microscopy, fluorescence microscopy, colorimetry, photobleaching, polarography, among others. The monograph is very useful for researchers and graduate students specializing in mitochondrial biophysics, biochemistry, molecular biology and cytology. The book was published in Russian in 2019 by Photon Publishers (Pushchino, Moscow region).
988 _aPrimersemestre_2020_BiomedLife
650 7 _2embne
_9147980
_aMitocondrias
773 0 _tSpringer eBooks
776 0 8 _iPrinted edition:
_z9783030338527
776 0 8 _iPrinted edition:
_z9783030338541
776 0 8 _iPrinted edition:
_z9783030338558
856 4 0 _uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://doi.org/10.1007/978-3-030-33853-4
_zAcceso a este recurso digital (usuarios Universidad Europea de Madrid)
942 _2lcc
_cLE
_n0
998 _b03/2020
_dz
_ek
_zSI