Roderich Brandsch

Roderich Brandsch

apl. Prof. em. Dr. rer. nat. (PhD)

Institute of Biochemistry and Molecular Biology
ZBMZ
Stefan-Meier-Str. 17
D-79104 Freiburg i. Br., Germany
+49(0)761-2035231
e-mail: roderich.brandsch@biochemie.uni-freiburg.de

CV

Academic training:	1961-1966	Diploma of the Faculty of Biology, University „A. I. Cuza”. Iasi, Romania
	1973	Dr. rer. nat. (PhD), University “A. I. Cuza” Iasi
	1974-1975	PostDoc., Fulbright-Hays Fellow at the Roche Institute of Molecular Biology, Department of Biochemistry, Nutley, NJ, USA
	1985	DAAD-fellow of the Gentechnology Program at the Department of Medical Biochemistry, Prof. Dr. K. N. Timmis, Genève, Switzerland
	1987	DAAD-fellow at the Roche Institute of Molecular Biology, Department of Dr. Herbert Weissbach, Nutley, N.J., USA
	1987	EMBO-fellow at the Institute of Microbiology, University of Lund, Sweden
Professional career:
	1966-1974	Researcher at the Biological Research Centre of the Romanian Academy of Sciences. Department of Physiology, Iasi, Romania
	1976-1980	Group leader at the Biological Research Centre
	1981	University Assistant at the Institute of Biochemistry, Albert-Ludwigs-University, Department Prof. Karl Decker
	1987	Habilitation in Biochemistry and Venia legendi of the MedicalFaculty of the Albert-Ludwigs-University, Freiburg, Germany
	1993-2008	Asociated Professor and Group Leader at the Institute of Biochemistry and Molecular Biology, Albert-Ludwigs University, Freiburg, Germany
	Since 2008	Emeritus at the Institute of Biochemistry and Molecular Biology

Research

Biochemical function and structure of enzymes of nicotine and carbohydrate catabolism encoded on the catabolic megaplasmid pOA1 of Arthrobacter nicotinovorans.

Fig. 1. Genome of the catabolic megaplasmid pAO1 of A. nicotinovorans

Fig. 2. Enzymes and intermediates of nicotine catabolism by A. nicotinovorans

Fig. 3. The nic-gene cluster of pAO1

Fig. 4. Comparison of nic-gene clusters of different bacterian

Reviews and book contributions

Ganas P, Igloi G L, Brandsch R (2009) The megaplasmid pAO1 of Arthrobacter

nicotinovorans and nicotine catabolism. Microbial Megaplasmids. Microbiology

Monographs 11 (ed. A. Steinbüchel) Springer-Verlag. Berlin

Brandsch R. (2006) Microbiology and biochemistry of nicotine degradation. Appl

Microbiol Biotechnol. 69:493-8.

Decker K, Brandsch R. (1997) Determining covalent flavinylation. Methods

Enzymol.280:413-23.

Brandsch R. (1994) Regulation of gene expression by cofactors derived from B vitamins.

J Nutr Sci Vitaminol 40:371-99. Review.

Decker K, Brandsch R. (1991) Flavoproteins with a covalent histidyl(N3)-8 alpha-

riboflavin linkage. Biofactors. 3:69-81. Review.

Pestka S, Baily L, Brandsch R, Graves P, Green M, Jilka R, McInnes J, Okuyama A, Tucker P, Weiss D, Yaffe L, Zehavi-Willner R.

(1976) Isolation, purification and cell-free

translation of immunoglobulin messenger RNAs from immunoglobulin producing

cells and variants. In: Immune RNA in Neoplasia (M A Fink, ed.), p. 121, Academic

Press, New York –San Francisco – London

Publications

bacterial nicotine catabolism

Hritcu L., Stefan M., Brandsch R and Mihasan M. (2015) Enhanced behavioral response by decreasing brain oxidative stress to 6-hydroxy-L-nicotine in Alzheiner’s disease rat model. Neuroscience Letters 591: 41 – 47

Mihasan M. and Brandsch R. (2013) pAO1 of Arthrobacter nicotinovorans and the spread of catabolic traits by horizontal gene transfer in Gram-positive soil bacteria. J Mol Evol 77: 22-30

Hritcu L., Stefan M., Brandsch R. and Mihasan M. (2013) 6-Hydroxy-L-nicotine from Arthrobacter nicotinovorans sustain spatial memory formation by decreasing brain oxidative stress in rats. J Physiol Biochem 69: 25-34

Cobzaru C., Ganas P., Mihasan M., Schleberger P., Brandsch R. (2011) Homologous gene clusters of nicotine catabolism, including a new ω-amidase for α-ketoglutaramate, in species of three genera of Gram-positive bacteria. Res Microbiol 162: 285-291

Mihasan M., Artenie V., Brandsch R . (2010) Cloning and purification of a tetrameric oxidoreductase from Arthrobacter nicotinovorans pAO1. An. Stiin.Univ. “A. I. Cuza” TOM XI: 1-6

Ganas P. and Brandsch R. (2009) Uptake of L-nicotine and of 6-hydroxy-L-nicotine by Arthrobacter nicotinovorans and by Escherichia coli is mediated by facilitated diffusion and not by passive diffusion or active transport. Microbiology 155: 1866-1877

Ganas P., Sachelaru P., Mihasan M., Igloi G. L., Brandsch R. (2008) Two closely related pathways of nicotine catabolism in Arthrobacter nicotinovorans and Nocardioides sp. strain JS614. Arch Microbiol 189:511-7

Ganas P., Mihasan M., Igloi G. L., Brandsch R. (2007) A two-component small multidrug resistance pump functions as a metabolic valve during nicotine catabolism by Arthrobacter nicotinovorans. Microbiology 153:1546-55

Mihasan M., Chiribau C. B., Friedrich T., Artenie V., Brandsch R. (2007) An NAD(P)H-nicotine blue oxidoreductase is part of the nicotine regulon and may protect Arthrobacter nicotinovorans from oxidative stress during nicotine catabolism. Appl Environ Microbiol 73:2479-85

Schleberger C., Sachelaru P., Brandsch R., Schulz G. E. (2007) Structure and action of a C-C bond cleaving alpha/beta-hydrolase involved in nicotine degradation. J Mol Biol 367:409-18

Sachelaru P., Schiltz E., Brandsch R. (2006) A functional mobA gene for molybdopterin cytosine dinucleotide cofactor biosynthesis is required for activity and holoenzyme assembly of the heterotrimeric nicotine dehydrogenases of Arthrobacter nicotinovorans. Appl Environ Microbiol 72:5126-31

Chiribau C. B., Mihasan M., Ganas P., Igloi G. L., Artenie V., Brandsch R. (2006) Final steps in the catabolism of nicotine. FEBS J 273:1528-36

Sandu C., Chiribau C. B., Sachelaru P., Brandsch R. (2005) Plasmids for nicotine-dependent and -independent gene expression in Arthrobacter nicotinovorans and other arthrobacter species. Appl Environ Microbiol 71:8920-4

Sachelaru P., Schiltz E., Igloi G. L., Brandsch R. (2005) An alpha/beta-fold C–C bond hydrolase is involved in a central step of nicotine catabolism by Arthrobacter nicotinovorans. J Bacteriol 187:8516-9

Chiribau C. B., Sandu C , Igloi G. L., Brandsch R. (2005) Characterization of PmfR, the transcriptional activator of the pAO1-borne purU-mabO-folD operon of Arthrobacter nicotinovorans. J Bacteriol 187:3062-70

Chiribau C. B., Sandu C., Fraaije M., Schiltz E., Brandsch R. (2004) A novel gamma-N-methylaminobutyrate demethylating oxidase involved in catabolism of the tobacco alkaloid nicotine by Arthrobacter nicotinovorans pAO1. Eur J Biochem 271:4677-84

Sandu C., Chiribau C. B., Brandsch R. (2003) Characterization of HdnoR, the transcriptional repressor of the 6-hydroxy-D-nicotine oxidase gene of Arthrobacter nicotinovorans pAO1, and its DNA-binding activity in response to L- and D-nicotine Derivatives. J Biol Chem. 278:51307-15

Sandu C. and Brandsch R. (2002) Evidence for MoeA-dependent formation of the molybdenum cofactor from molybdate and molybdopterin in Escherichia coli. Arch Microbiol. 178:465-70

Sandu C, Brandsch R. (2002) Functional analysis of the Escherichia coli molybdopterin cofactor biosynthesis protein MoeA by site-directed mutagenesis. Biol Chem 383(2):319-23

Baitsch D., Sandu C., Brandsch R., Igloi G. L. (2001) Gene cluster on pAO1 of Arthrobacter nicotinovorans involved in degradation of the plant alkaloid nicotine: cloning, purification, and characterization of 2,6-dihydroxypyridine 3-hydroxylase. J Bacteriol 183:5262-7

Sandu C., Nick P., Hess D., Schiltz E., Garrow T. A., Brandsch R. (2000) Association of betaine-homocysteine S-methyltransferase with microtubules. Biol Chem 381:619-622

Menéndez C., Otto A., Igloi G., Nick P., Brandsch R., Schubach B., Böttcher B., Brandsch R. (1997) Molybdate-uptake genes and molybdopterin-biosynthesis genes on a bacterial plasmid–characterization of MoeA as a filament-forming protein with adenosinetriphosphatase activity. Eur J Biochem 250:524-31

Grether-Beck S., Igloi G. L., Pust S., Schilz E., Decker K., Brandsch R. (1994) Structural analysis and molybdenum-dependent expression of the pAO1-encoded nicotine dehydrogenase genes of Arthrobacter nicotinovorans. Mol Microbiol 13:929-936

Bernauer H., Mauch L., Brandsch R. (1992) Interaction of the regulatory protein NicR1 with the promoter region of the pAO1-encoded 6-hydroxy-D-nicotine oxidase gene of Arthrobacter oxidans. Mol Microbiol 6:1809-20

Mauch L., Bichler V., Brandsch R. (1990) Functional analysis of the 5′ regulatory region and the UUG translation initiation codon of the Arthrobacter oxidans 6-hydroxy-D-nicotine oxidase gene. Mol Gen Genet 221:427-34

Brandsch R., Hinkkanen A. E., Mauch L., Nagursky H., Decker K. (1987) 6-Hydroxy-D-nicotine oxidase of Arthrobacter oxidans. Gene structure of the flavoenzyme and its relationship to 6-hydroxy-L-nicotine oxidase. Eur J Biochem 167:315-20

Brandsch R. and Decker K. (1982) The effect of gyrase inhibitors and cyclic AMP on induction and glucose repression of the 6-hydroxy-nicotine oxidases in Arthrobacter oxidans. Arch Microbiol 133:274-7

megaplasmid pAO1; horizontal gene transfer

Mihasan, M. and Brandsch, R. (2016) A predicted T4 secretion system and conserved DNA-repeats identified in a subset of related Arthrobacter plasmids. Microbiol Res. 191: 12-37

Mihasan M. and Brandsch R. (2013) pAO1 of Arthrobacter nicotinovorans and the spread of catabolic traits by horizontal gene transfer in Gram-positive soil bacteria. J Mol Evol 77: 22-30

Mihasan M., Stefan M., Hritcu L., Artenie V. and Brandsch R. (2013) Evidence of plasmid-encoded oxidative xylose-catabolic pathway in Arthrobacter nicotinovorans pAO1. Res Microbiol 164: 22-30

Ganas P, Igloi G L, Brandsch R (2009) The megaplasmid pAO1 of Arthrobacter

nicotinovorans and nicotine catabolism. Microbial Megaplasmids. Microbiology

Monographs 11 (ed. A. Steinbüchel) Springer-Verlag. Berlin

Sandu C., Chiribau C. B., Sachelaru P., Brandsch R. (2005) Plasmids for nicotine-dependent and -independent gene expression in Arthrobacter nicotinovorans and other Arthrobacter species. Appl Environ Microbiol 71:8920-4

Igloi G. Ll and Brandsch R. (2003) Sequence of the 165-kilobase catabolic plasmid pAO1 from Arthrobacter nicotinovorans and identification of a pAO1-dependent nicotine uptake system. J Bacteriol.185:1976-86

Menéndez C., Igloi G. L., Brandsch R. (1997) IS1473, a putative insertion sequence identified in the plasmid pAO1 from Arthrobacter nicotinovorans: isolation, characterization, and distribution among Arthrobacter species. Plasmid 37:35-41

Menéndez C., Siebert D., Brandsch R. (1996) MoaA of Arthrobacter nicotinovorans pAO1 involved in Mo-pterin cofactor synthesis is an Fe-S protein. FEBS Lett 391:101-3

Menéndez C., Igloi G., Henninger H., Brandsch R. (1995) A pAO1-encoded molybdopterin cofactor gene (moaA) of Arthrobacter nicotinovorans: characterization and site-directed mutagenesis of the encoded protein. Arch Microbiol 164:142-51

Brandsch R., Faller W., Schneider K. (1986) Plasmid pAO1 of Arthrobacter oxidans encodes 6-hydroxy-D-nicotine oxidase: cloning and expression of the gene in Escherichia coli. Mol Gen Genet 202:96-101

Brandsch R. and Decker K. (1984) Isolation and partial characterization of plasmid DNA from Arthrobacter oxidans. Arch Microbiol.138:15-7

Brandsch R., Hinkkanen A. E., Decker K. (1982) Plasmid-mediated nicotine degradation in Arthrobacter oxidans. Arch Microbiol 132:26-30

Brandsch R., Hefco E. Brandsch C., Rotinberg P., Kelemen S. (1980) Possible plasmid control of sporulation, soluble pigment production and tetracycline resistance in a wild Streptomyces sp. strain. J Antibiot 33:1204-5

autoflavinylation (6HDNO; DMGDH)

Hritcu L, Stefan M, Brandsch R, Mihasan M. (2015) Enhanced behavioral response by decreasing brain oxidative stress to 6-hydroxy-l-nicotine in Alzheimer’s disease rat model. Neurosci Lett. 591:41-7.

Giancaspero TA, Colella M, Brizio C, Difonzo G, Fiorino GM, Leone P, Brandsch R, Bonomi F, Iametti S, Barile M. (2015) Remaining challenges in cellular flavin cofactor homeostasis and flavoprotein biogenesis. Front. Chem. 30: 1-14

Brizio C., Brandsch R., Douka M., Wait R., Barile M. (2008) The purified recombinant precursor of rat mitochondrial dimethylglycine dehydrogenase binds FAD via an autocatalytic reaction. Int J Biol Macromol 42:455-462

Brizio C., Brandsch R., Bufano D., Pochini L., Indiveri C., Barile M. (2004) Over-expression in Escherichia coli, functional characterization and refolding of rat dimethylglycine dehydrogenase. Protein Expr Purif. 37:434-42

Brizio C., Barile M., Brandsch R. (2002) Flavinylation of the precursor of mitochondrial dimethylglycine dehydrogenase by intact and solubilised mitochondria. FEBS Lett 522:141-146

Brizio C., Otto A., Brandsch R., Passarella S., Barile M. (2000) A protein factor of rat liver mitochondrial matrix involved in flavinylation of dimethylglycine dehydrogenase. Eur J Biochem 267:4346-54

Bergeron F., Otto A., Blache P., Day R., Denoroy L., Brandsch R., Bataille D. (1998) Molecular cloning and tissue distribution of rat sarcosine dehydrogenase. Eur J Biochem 257:556-61

Stoltz M. and Brandsch R. (1998) The conformational change induced by FAD in covalently flavinylated 6-hydroxy-D-nicotine oxidase does not require (8alpha)FAD-(N3)histidyl bond formation. J Biochem 123:445-9

Stoltz M., Rassow J., Bückmann A. F., Brandsch R. (1996) Covalent attachment of FAD derivatives to a fusion protein consisting of 6-hydroxy-D-nicotine oxidase and a mitochondrial presequence. Folding, enzyme activity, and import of the modified protein into yeast mitochondria. J Biol Chem 271:25208-12

Stoltz M., Henninger H. P., Brandsch R. (1996) The design of an alternative, covalently flavinylated 6-hydroxy-D-nicotine oxidase by replacing the FAD-binding histidine by cysteine and reconstitution of the holoenzyme with 8-(methylsulfonyl)FAD. FEBS Lett. 386:194-6

Otto A., Stoltz M., Sailer H. P., Brandsch R. (1996) Biogenesis of the covalently flavinylated mitochondrial enzyme dimethylglycine dehydrogenase. J Biol Chem 271:9823-9

Stoltz M., Rysavy P., Kalousek F., Brandsch R. (1995) Folding, flavinylation, and mitochondrial import of 6-hydroxy-D-nicotine oxidase fused to the presequence of rat dimethylglycine dehydrogenase. J Biol Chem 270:8016-22

Lang H., Minaian K., Freudenberg N., Hoffmann R., Brandsch R. (1994) Tissue specificity of rat mitochondrial dimethylglycine dehydrogenase expression. Biochem J 299:393-8

Brandsch R., Bichler V., Mauch L., Decker K. (1993) Cysteine to serine replacements in 6-hydroxy-D-nicotine oxidase. Consequences for enzyme activity, cofactor incorporation, and formation of high molecular weight protein complexes with molecular chaperones (GroEL). J Biol Chem 268:12724-9

Brandsch R., Bichler V., Schmidt M., Buchner J. (1992) GroE dependence of refolding and holoenzyme formation of 6-hydroxy-D-nicotine oxidase. J Biol Chem 267:20844-20849

Brandsch R. and Bichler V. (1991) Autoflavinylation of apo6-hydroxy-D-nicotine oxidase. J Biol Chem 266:19056-62

Lang H., Polster M., Brandsch R. (1991) Rat liver dimethylglycine dehydrogenase. Flavinylation of the enzyme in hepatocytes in primary culture and characterization of a cDNA clone. Eur J Biochem. 198:793-9

Brandsch R. and Bichler V. 1990 Riboflavin-dependent expression of flavoenzymes of the nicotine regulon of Arthrobacter oxidans. Biochem J 270:673-8

Mauch L., Bichler V., Brandsch R. (1990) Lysine can replace arginine 67 in the mediation of covalent attachment of FAD to histidine 71 of 6-hydroxy-D-nicotine oxidase. J Biol Chem 265:12761-2

Mauch L., Bichler V., Brandsch R. (1989) Site-directed mutagenesis of the FAD-binding histidine of 6-hydroxy-D-nicotine oxidase. Consequences on flavinylation and enzyme activity. FEBS Lett 257:86-8

Brandsch R., Hederstedt L. (1989) Expression and flavinylation of Arthrobacter oxydans 6-hydroxy-D-nicotine oxidase in Bacillus subtilis. J Gen Microbiol 135: 1093-1099

Brandsch R. and Bichler V. (1989) Covalent cofactor binding to flavoenzymes requires specific effectors. Eur J Biochem 182:125-8

Brandsch R., Bichler V, Krauss B. (1989) Binding of FAD to 6-hydroxy-D-nicotine oxidase apoenzyme prevents degradation of the holoenzyme. Biochem J. 258:187-92

Nagursky H., Bichler V., Brandsch R. (1988) Phosphoenolpyruvate-dependent flavinylation of 6-hydroxy-D-nicotine oxidase. Eur J Biochem 177:319-25

Brandsch R. and Bichler V. (1987) Covalent flavinylation of 6-hydroxy-D-nicotine oxidase involves an energy-requiring process. FEBS Lett. 224:121-4

Brandsch R., Bichler V., Nagursky H. (1987) Covalent flavinylation of 6-hydroxy-D-nicotine oxidase analyzed by partial deletions of the gene. Eur J Biochem. 165:559-64

Brandsch R. and Bichler V. (1986) Studies in vitro on the flavinylation of 6-hydroxy-D-nicotine oxidase. Eur J Biochem 160:285-9

Brandsch R. and Bichler V. (1985) In vivo and in vitro expression of the 6-hydroxy-D-nicotine oxidase gene of Arthrobacter oxidans, cloned into Escherichia coli, as an enzymatically active, covalently flavinylated polypeptide. FEBS Lett 192:204-8

Swafford JR, Reeves HC, Brandsch R. (1985) Localization of the enantiozymes of 6-hydroxy-nicotine oxidase in Arthrobacter oxidans by electron immunochemistry. J Bacteriol 163:792-795

anti-flavin antibodies in myocarditis

Cicek G., Schiltz E., Staiger J., Neumann F. J., Melchers I., Brandsch R. (2003) Specific stimulation of peripheral blood mononuclear cells from patients with acute myocarditis by peptide-bound flavin adenine dinucleotide (FAD), a naturally occurring autologous hapten. Clin Exp Immunol 132:366-70

Cicek G., Schiltz E., Hess D., Staiger J., Brandsch R.(2002) Analysis of mitochondrial antigens reveals inner membrane succinate dehydrogenase flavoprotein subunit as autoantigen to antibodies in anti-M7 sera. Clin Exp Immunol 128:83-87

Cicek G., Vuorinen T., Stähle I., Stepanek P., Freudenberg N., Brandsch R.(2000) Coxsackievirus B3 infection induces anti-flavoprotein antibodies in mice. Clin Exp Immunol 122:404-9

Stähle I., Brizzio C., Barile M., Brandsch R. (1999) Anti-mitochondrial flavoprotein autoantibodies of patients with myocarditis and dilated cardiomyopathy (anti-M7): interaction with flavin-carrying proteins, effect of vitamin B2 and epitope mapping. Clin Exp Immunol 115:404-8.

Otto A., Stähle I., Klein R., Berg P. A., Pankuweit S., Brandsch R. (1998) Anti-mitochondrial antibodies in patients with dilated cardiomyopathy (anti-M7) are directed against flavoenzymes with covalently bound FAD. Clin Exp Immunol 111:541-7

miscellaneous

Brandsch R., Brandsch Cs., Sauciuc A., Duca E., Rotinberg P., Kelemen S. (1980) Effect of chemically modified nystatine in association with actinomycin D and puromycin on Hela cell polysomal profiles. Rev Roum Biologie-Zoologie 25: 63-68

Simionescu C. I., Denes F., Brandsch R. (1979) Biological and biochemical activities of protobiopolymers. J Polymer Science. 66:117-128

Brandsch R., Hefco E., Iluc E. (1978) Isolation and characterization of plasmid DNA from a wild Streptomyces strain. Trav Mus Hist Nat “Grigore Antipa” 3: 126-132

Brandsch R, Rotinberg P, Brandsch Cs, Kelemen S. (1978) Identification of subfractions within ribonucleoprotein particles derived from polysomes. Rev Roum Biologie-Zoologie 23:169-174

Omura S., Nakagawa A., Sakakibara H., Okekawa O., Brandsch R., Pestka S. (1977) Structure-activity relationships among the O-acyl derivatives of leucomycin. Correlation of minimal inhibitory concentrations with binding to Escherichia coli ribosomes. J Med Chem. 20:732-6

Jitariu P., Pavelescu-Schneller C., Brandsch R. (1973) May the electromagnetic field be regarded as an environmental factor? Rev Roum Biologie-Zoologie 18: 227-234

Brandsch R. and Brandsch Cs. (1973) Cell division and growth response in root tips of Allium cepa and Secale cereale in magnetic fields. Rev Roum Biologie-Zoologie 18: 145-152

Brandsch R. (1972) Cleavage of Tubifex eggs under various conditions of magnetic field applied at different periods of the cell cycle. Rev Roum Biologie-Zoologie 17: 121-129

Brandsch R. and Jitariu P. (1971) Influence of colchicine and theophiline combined with an electromagnetic field on the first cleavage divisions of Tubifex eggs. Rev Roum Biologie-Zoologie 16: 215-220

Brandsch R. and Jitariu P. (1970) Der Einfluss eines pulsierenden elektromagnetischen Feldes auf die Entwicklung und die ersten Furchungsteilungen der Embryonen von Tubifex tubifex. Rev Roum Biologie-Zoologie 15: 431-436.

Artenie V., Brandsch R., Duca E., Hefco E., Link F., Jitariu M. (1971) Vitamin C and glucose metabolism in the early stages of embryogenesis in Salmo Gaidneri. Rev Roum Biologie-Zoologie 16: 189-193

Jitariu M., Artenie V., Badilita M., Brandsch R., Duca E., Hefco E. (1970) La vitamine C et le metabolism du glucose dans les stades primordiaux de l’embriogenese de Salmo trutta fario. Rev Roum Biologie-Zoologie 15: 267-272

Jitariu M., Hefco E., Müller W., Badilita M., Duca E., Brandsch R., Boisteanu R., Davideanu G. (1969) Some metabolic aspects of the carotenoid substances in embrionary development in Salmonides. Comp. Physiol. Anim. 14, 190-194

Tudose I. and Brandsch R. (1969) Die Beeinflussung der Entwicklung von Drosophila melanogaster durch Ephedrin und seine Wirkung auf die Speicheldrüsenchromosomen. Cercetari de genetica II: 404-407

Jitariu P., Hefco V., Birca D., Brandsch R. (1968) Der Einfluss von Magnetfeldern auf den Stoffwechsel der Kohlenhydrate. Anal St “Univ Al I Cuza” Iasi, Biologie 14: 7-13.

Back