Leopold Flohé

ORCID: 0000-0003-0940-8179
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About
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Research Areas
  • Selenium in Biological Systems
  • Redox biology and oxidative stress
  • Research on Leishmaniasis Studies
  • Sulfur Compounds in Biology
  • Organoselenium and organotellurium chemistry
  • Glutathione Transferases and Polymorphisms
  • Trypanosoma species research and implications
  • Trace Elements in Health
  • Enzyme function and inhibition
  • Protease and Inhibitor Mechanisms
  • Insect and Pesticide Research
  • Neutrophil, Myeloperoxidase and Oxidative Mechanisms
  • Sperm and Testicular Function
  • Hemoglobin structure and function
  • Amino Acid Enzymes and Metabolism
  • Environmental Toxicology and Ecotoxicology
  • Free Radicals and Antioxidants
  • Synthesis and Biological Evaluation
  • Parasites and Host Interactions
  • Synthesis and Characterization of Heterocyclic Compounds
  • Enzyme Production and Characterization
  • Vitamin C and Antioxidants Research
  • Electron Spin Resonance Studies
  • Hormonal and reproductive studies
  • Nitric Oxide and Endothelin Effects

University of Padua
1974-2024

München Klinik Schwabing
2024

Technical University of Munich
1987-2024

Universidad de la República de Uruguay
2014-2023

Universidad de Montevideo
2015

Otto-von-Guericke University Magdeburg
2009-2013

Mundipharma (United Kingdom)
2005-2007

Technische Universität Braunschweig
1996-2006

University Hospital Magdeburg
2005

Helmholtz Centre for Infection Research
1991-2003

10.1016/s0076-6879(84)05015-1 article EN Methods in enzymology on CD-ROM/Methods in enzymology 1984-01-01

10.1016/s0076-6879(84)05013-8 article EN Methods in enzymology on CD-ROM/Methods in enzymology 1984-01-01

The selenoprotein phospholipid hydroperoxide glutathione peroxidase (PHGPx) changes its physical characteristics and biological functions during sperm maturation. PHGPx exists as a soluble in spermatids but persists mature spermatozoa an enzymatically inactive, oxidatively cross-linked, insoluble protein. In the midpiece of spermatozoa, protein represents at least 50 percent capsule material that embeds helix mitochondria. role structural may explain mechanical instability mitochondrial is...

10.1126/science.285.5432.1393 article EN Science 1999-08-27

Selenoprotein P (SePP), the major selenoprotein in plasma, has been implicated selenium transport, detoxification or antioxidant defence. We generated SePP-knockout mice that were viable, but exhibited reduced growth and developed ataxia. Selenium content was elevated liver, low plasma other tissues, selenoenzyme activities changed accordingly. Our data reveal SePP plays a pivotal role delivering hepatic to target tissues.

10.1042/bj20021853 article EN Biochemical Journal 2003-02-24

Article An Improved Coupled Test Procedure for Glutathione Peroxidase (EC 1.11.1.9.) in Blood was published on January 1, 1974 the journal Clinical Chemistry and Laboratory Medicine (CCLM) (volume 12, issue 10).

10.1515/cclm.1974.12.10.444 article EN Clinical Chemistry and Laboratory Medicine (CCLM) 1974-01-01

10.1515/bchm2.1972.353.1.987 article EN Hoppe-Seyler´s Zeitschrift für physiologische Chemie 1972-01-01

The complete sequence of 157 amino acids the light (A) chain high molecular mass urokinase from human urine was determined. fragmentation strategy included cyanogen bromide cleavage S-carboxymethylated A at methionine and/or tryptophan residues and use specific endoproteinase Lys-C. For determination automated solid- or liquid-phase techniques Edman degradation were used. C-terminal determined by consecutive treatment with carboxypeptidase B. acid obtained revealed a significant homology to...

10.1515/bchm2.1982.363.2.1155 article EN Hoppe-Seyler´s Zeitschrift für physiologische Chemie 1982-01-01

The human genome contains 25 genes coding for selenocysteine-containing proteins (selenoproteins). These are involved in a variety of functions, most notably redox homeostasis. Selenoprotein enzymes with known functions designated according to these functions: TXNRD1, TXNRD2, and TXNRD3 (thioredoxin reductases), GPX1, GPX2, GPX3, GPX4, GPX6 (glutathione peroxidases), DIO1, DIO2, DIO3 (iodothyronine deiodinases), MSRB1 (methionine sulfoxide reductase B1), SEPHS2 (selenophosphate synthetase...

10.1074/jbc.m116.756155 article EN cc-by Journal of Biological Chemistry 2016-09-20

Abstract Lipoic acid (thiotic acid) is being used as a dietary supplement, and therapeutic agent, reported to have beneficial effects in disorders associated with oxidative stress, but its mechanism of action remains unclear. We present evidence that lipoic induces substantial increase cellular reduced glutathione cultured human Jurkat T cells, erythrocytes, C6 glial NB41A3 neuroblastoma peripheral blood lymphocytes. The effect depends on metabolic reduction dihydrolipoic acid. Dihydrolipoic...

10.1002/biof.5520060303 article EN BioFactors 1997-01-01

The selenoprotein phospholipid hydroperoxide glutathione peroxidase (PHGPx) accounts for almost the entire selenium content of mammalian testis. PHGPx is abundantly expressed in spermatids as active but transformed to an oxidatively inactivated protein mature sperm, where it a major constituent mitochondrial capsule midpiece. Male infertility selenium-deficient animals, which characterized by impaired sperm motility and morphological midpiece alterations, considered result from insufficient...

10.1095/biolreprod.102.003822 article EN Biology of Reproduction 2002-09-01

Parasitic trypanosomatids comprise causative agents of debilitating or life-threatening tropical diseases. The limited capacity these parasites to cope with oxidative stress has been discussed as a target area for therapeutic approaches but success hampered by lack comprehension their peculiar oxidant defense system depending on the unique redox metabolite trypanothione. Here we report that trypanothione-dependent hydroperoxide metabolism in Crithidia fasciculata is catalysed two distinct...

10.1515/bchm.1997.378.8.827 article EN Biological Chemistry 1997-01-01

Single and double site mutants affecting the presumed catalytic centre of selenoenzyme PHGPx were subjected to functional analysis. The rate constants k+1 k'+2, for oxidation regeneration ground state enzyme estimated, respectively. Moreover, alkylation reactive by iodoacetate (kinact.) was also analysed. substitution catalytically competent selenocysteine 46 cysteine (PHGPxcys46) decreased k'+2 about three orders magnitude, although leaving unaffected kinact.. Furthermore, mutations...

10.1515/bchm3.1995.376.11.651 article EN Biological Chemistry Hoppe-Seyler 1995-01-01
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