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Acta Biologica et Medica Germanica. Band 38, Heft 2/3 / hrsg. von R. Baumann.

Contributor(s): Material type: TextTextSeries: Acta Biologica et Medica Germanica ; Band 38, Heft 2/3Publisher: Berlin ; Boston : De Gruyter, [2022]Copyright date: 1979Edition: Reprint 2022Description: 1 online resource (420 p.)Content type:
Media type:
Carrier type:
ISBN:
  • 9783112650059
  • 9783112650066
Subject(s): DDC classification:
  • 500
LOC classification:
  • QD116.P68 .G756 1979
Other classification:
  • online - DeGruyter
Online resources: Available additional physical forms:
  • Issued also in print.
Contents:
Frontmatter -- INHALTSVERZEICHNIS -- SACHWORTVERZEICHNIS -- AUTORENVERZEICHNIS -- Preface -- A thermodynamic-kinetic analysis of the cytochrome P-450 heme pocket -- Cytochrome P-450Cam and putidaredoxin interaction during electron transfer -- Spin state transitions of liver microsomal cytochrome P-450 -- Quantitative analysis of the spin equilibrium of cytochrome P-450 LM2 fraction from rabbit liver microsomes -- The importance of the spin equilibrium in cytochrome P-450 for the reduction rate of the heme iron -- Activated forms of oxygen in the metabolism of xenobiotics catalyzed by cytochrome P-450 -- Comparison of spectral properties of 3-MC induced cytochrome P-448 from rabbits and rats -- Comparison of microsomal and solubilized monooxygenases from rat and rabbit by proton magnetic relaxation -- Stereochemical properties of the binding site of liver microsomal cytochrome P-450 as studied by substrate analogous spin labels -- Infrared spectral studies of carbon monoxide complexes of microsomal cytochromes P-450 and P-448 -- Isolation, structural organization and mechanism of action of mitochondrial steroid hydroxylating systems -- Molecular properties of cytochrome P-45011/3 from adrenal cortex mitochondria -- Model systems for the coordination chemistry of cytochrome P-450 -- The properties of cytochrome P-450 and hydroxylase activity of reconstituted pfoteoliposomal membranes -- Pituitary control of hepatic steroid metabolism -- Gas chromatography-mass spectrometry in analysis of protein amino acid composition -- Isolation and characterization of cytochrome P-450meg -- The alkane-hydroxylating enzyme system of the yeast Candida guilliermondii -- Mercaptide chelated protoheme : A model compound for cytochrome P-450 -- The role of metal ions in oxygen activation -- Quantum chemical interpretation of the spectral properties of the GO and Oa complexes of hemoglobin and cytochrome P-450 -- Catalytic properties of the liver microsomal hydroxylase system in reconstituted phospholipid vesicles -- Hydrodynamic studies on interactions between the components of the liver microsomal cytochrome P-450 system -- NADPH reduction of cytochrome P-450 at different integrational levels of the enzyme system -- Enzymatic activities of matrix-bound components of the liver microsomal cytochrome P-450 system -- Oxycytochrome P-450 : Its breakdown to superoxide for the formation of hydrogen peroxide -- NADPH-dependent electron transport chain in microsomes and lipid peroxidation catalyzed by metal ions -- Spectral properties of nonequilibrium states in cytochrome P-450 formed by reduction at subzero temperatures -- Mechanistic studies with purified components of the liver microsomal hydroxylation system: Spectral intermediates in reaction of cytochrome P-450 with peroxy compounds -- Kinetics of reduction of purified liver microsomal cytochrome P-450 in the reconstituted enzyme system studied by stopped flow spectrophotometry -- Electronic and steric factors in regioselective hydroxylation catalyzed by purified cytochrome P-450 -- Interaction of cytochrome P-450 with hydrocarbons -- Comparison of the peroxidatic activity of cytochrome P-450 with other hemoproteins and model compounds -- Electrochemical investigations on the oxygen activation by cytochrome P-450 -- The mechanism of hydroperoxide-dependent reactions with participation of cytochrome P-450 -- CONTENTS
Holdings
Item type Current library Call number URL Status Notes Barcode
eBook eBook Biblioteca "Angelicum" Pont. Univ. S.Tommaso d'Aquino Nuvola online online - DeGruyter (Browse shelf(Opens below)) Online access Not for loan (Accesso limitato) Accesso per gli utenti autorizzati / Access for authorized users (dgr)9783112650066

Frontmatter -- INHALTSVERZEICHNIS -- SACHWORTVERZEICHNIS -- AUTORENVERZEICHNIS -- Preface -- A thermodynamic-kinetic analysis of the cytochrome P-450 heme pocket -- Cytochrome P-450Cam and putidaredoxin interaction during electron transfer -- Spin state transitions of liver microsomal cytochrome P-450 -- Quantitative analysis of the spin equilibrium of cytochrome P-450 LM2 fraction from rabbit liver microsomes -- The importance of the spin equilibrium in cytochrome P-450 for the reduction rate of the heme iron -- Activated forms of oxygen in the metabolism of xenobiotics catalyzed by cytochrome P-450 -- Comparison of spectral properties of 3-MC induced cytochrome P-448 from rabbits and rats -- Comparison of microsomal and solubilized monooxygenases from rat and rabbit by proton magnetic relaxation -- Stereochemical properties of the binding site of liver microsomal cytochrome P-450 as studied by substrate analogous spin labels -- Infrared spectral studies of carbon monoxide complexes of microsomal cytochromes P-450 and P-448 -- Isolation, structural organization and mechanism of action of mitochondrial steroid hydroxylating systems -- Molecular properties of cytochrome P-45011/3 from adrenal cortex mitochondria -- Model systems for the coordination chemistry of cytochrome P-450 -- The properties of cytochrome P-450 and hydroxylase activity of reconstituted pfoteoliposomal membranes -- Pituitary control of hepatic steroid metabolism -- Gas chromatography-mass spectrometry in analysis of protein amino acid composition -- Isolation and characterization of cytochrome P-450meg -- The alkane-hydroxylating enzyme system of the yeast Candida guilliermondii -- Mercaptide chelated protoheme : A model compound for cytochrome P-450 -- The role of metal ions in oxygen activation -- Quantum chemical interpretation of the spectral properties of the GO and Oa complexes of hemoglobin and cytochrome P-450 -- Catalytic properties of the liver microsomal hydroxylase system in reconstituted phospholipid vesicles -- Hydrodynamic studies on interactions between the components of the liver microsomal cytochrome P-450 system -- NADPH reduction of cytochrome P-450 at different integrational levels of the enzyme system -- Enzymatic activities of matrix-bound components of the liver microsomal cytochrome P-450 system -- Oxycytochrome P-450 : Its breakdown to superoxide for the formation of hydrogen peroxide -- NADPH-dependent electron transport chain in microsomes and lipid peroxidation catalyzed by metal ions -- Spectral properties of nonequilibrium states in cytochrome P-450 formed by reduction at subzero temperatures -- Mechanistic studies with purified components of the liver microsomal hydroxylation system: Spectral intermediates in reaction of cytochrome P-450 with peroxy compounds -- Kinetics of reduction of purified liver microsomal cytochrome P-450 in the reconstituted enzyme system studied by stopped flow spectrophotometry -- Electronic and steric factors in regioselective hydroxylation catalyzed by purified cytochrome P-450 -- Interaction of cytochrome P-450 with hydrocarbons -- Comparison of the peroxidatic activity of cytochrome P-450 with other hemoproteins and model compounds -- Electrochemical investigations on the oxygen activation by cytochrome P-450 -- The mechanism of hydroperoxide-dependent reactions with participation of cytochrome P-450 -- CONTENTS

restricted access online access with authorization star

http://purl.org/coar/access_right/c_16ec

Issued also in print.

Mode of access: Internet via World Wide Web.

In German.

Description based on online resource; title from PDF title page (publisher's Web site, viewed 19. Oct 2024)