Výsledky vyhledávání - "Michael Lehnerer"

Residue 285 in Cytochrome P450 2B4 Lacking the NH2-Terminal Hydrophobic Sequence Has a Role in the Functional Association of NADPH–Cytochrome P450 Reductase

Autor: Johannes Schulze, Katharina Tschöp, Michael Lehnerer, Peter Hlavica

Publikováno v: Biochemical and Biophysical Research Communications. 270:777-781

Cytochrome P450 2B4 (CYP2B4) lacking the NH(2)-terminal signal anchor sequence (2-27) was used to study the impact of replacement of histidine with alanine at position 285 on electron transfer from NADPH-cytochrome P450 reductase (P450R). Absorption

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea364a8a4affec986bc25a3ce3437b9b
https://doi.org/10.1006/bbrc.2000.2495

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The Optical Biosensor Studies on the Role of Hydrophobic Tails of NADPH-Cytochrome P450 Reductase and Cytochromes P450 2B4 and b5 upon Productive Complex Formation within a Monomeric Reconstituted System

Autor: Yuri D. Ivanov, Alexander I. Archakov, Peter Hlavica, Vadim Yu. Kuznetsov, Michael Lehnerer, Johannes Schulze, Irina P. Kanaeva

Publikováno v: Archives of Biochemistry and Biophysics. 362:87-93

The optical biosensor study of interaction between microsomal proteins—NADPH-cytochrome P450 reductase, cytochrome P450 2B4, and cytochrome b5—was carried out in the monomeric reconstituted system in the absence of phospholipids. The formation of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02fdbde334db4d5576cafbb49dbdd4db
https://doi.org/10.1006/abbi.1998.0981

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Amino acid residue 250 has a functional role in the assembly of rabbit liver microsomal cytochrome P450 2B4

Autor: David F.V. Lewis, Peter Hlavica, Michael Lehnerer, Johannes Schulze

Publikováno v: IUBMB Life. 44:1147-1155

Cytochrome P450 2B4 lacking amino acids 2-27, CYP2B4 (delta2-27), was mutated at position 250 and expressed in E. coli fused to glutathione S-transferase. Expression of the E250S variant (holo- plus apoenzyme) proceeded to an extent comparable with t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86fa84e0b0746df95152b765b1ffc353
https://doi.org/10.1080/15216549800202232

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Primary aromatic amines: their N-oxidative bioactivation

Autor: Johannes Schulze, Peter Hlavica, I. Golly, Michael Lehnerer

Publikováno v: Human & Experimental Toxicology. 16:441-448

There exists a diversity of pathways in mammalian cells serving to activate primary aromatic amines. 1 N-Oxidative mixed-function turnover usually involves participation of the cytochrome P450 superfamily, while catalysis by the flavin-containing mon

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::daf3146305a9a2ce05ac7c3991d06c4c
https://doi.org/10.1177/096032719701600805

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An optical biosensor study of the interaction parameters and role of hydrophobic tails of cytochrome P450 2B4, b5 and NADPH-flavoprotein in complex formation

Autor: Johannes Schulze, Konstantin G. Sklyabin, Michail A. Eldarov, Yuriy D. Ivanov, Peter Hlavica, Irina P. Kanaeva, Alexander I. Archakov, Michael Lehnerer

Publikováno v: IUBMB Life. 42:731-737

The real-time interactions of membrane proteins - cytochrome P450 2B4, NADPH cytochrome P450 reductase and cytochrome b5 - were studied by use of an optical biosensor system. The association and dissociation rate constants for the individual complexe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::604686ea40646a60dd7cadf242ea3a93
https://doi.org/10.1080/15216549700203161

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Some aspects of the role of cytochrome P-450 isozymes in the n-oxidative transformation of secondary and tertiary amine compounds

Autor: Michael Lehnerer, Peter Hlavica

Publikováno v: Journal of Biochemical Toxicology. 10:275-285

Indirect evidence of the participation of cytochrome P-450 (P-450) in the microsomal N-oxygenation of secondary and tertiary nitrogen functions is presented by studies employing diagnostic modifiers of the hemoprotein system as well as antibodies dir

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bbc5193557cc177805eb762bd14e77d4
https://doi.org/10.1002/jbt.2570100508

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N-Oxidative Transformations of Cï£¾N Groups as Means of Toxification and Detoxification

Autor: Michael Lehnerer, Peter Hlavica

Publikováno v: Patai's Chemistry of Functional Groups

1 Introduction 2 Chemical Aspects of the N-Oxygenation of the CN Functionality 3 Occurrence of N-Oxygenated CN Functionalities in Natural and Synthetic Compounds and Biological Activity 4 Metabolic in Vivo and in Vitro Formation of N-Oxygenated CN Fu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a6ba4fc981807fda805ec4b8f20551b0
https://doi.org/10.1002/9780470682531.pat0143

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Mitochondrial malate dehydrogenase from watermelon: sequence of cDNA clones and primary structure of the higher-plant precursor protein

Autor: Ole Olsen, Christine Gietl, Michael Lehnerer

Publikováno v: Plant Molecular Biology. 14:1019-1030

The isolation and sequence of a cDNA clone encoding the complete mitochondrial malate dehydrogenase (mMDH) of watermelon cotyledons is presented. Taking advantage of the polymerase chain reaction technology partial cDNA clones from the central part,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab2b04d74f7fb0e955b7d7b73915f78f
https://doi.org/10.1007/bf00019398

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