G. Michel

Centre Hospitalier de Luxembourg

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F. Peypoux

Université Claude Bernard Lyon 1

Micheline Guinand

Université Claude Bernard Lyon 1

M. Bruneteau

Université Claude Bernard Lyon 1

Marie‐Jeanne Vacheron

Université Claude Bernard Lyon 1

F. Besson

Université Claude Bernard Lyon 1

E. Lederer

Institut de Chimie des Substances Naturelles

B.C. Das

Institut de Chimie des Substances Naturelles

Pierre Ricci

Institut Sophia Agrobiotech

Maryvonne Ciavatti

Inserm

L. Delcambe

National Centre for Research and Development

Cooperative Institutions

Centre National de la Recherche Scientifique

University College London

Université Claude Bernard Lyon 1

Inserm

Université Paris Cité

Sorbonne Université

Laboratoire de Chimie

Assistance Publique – Hôpitaux de Paris

Commissariat à l'Énergie Atomique et aux Énergies Alternatives

Institut National de la Recherche Agronomique

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Isolation identification and biological activity of phospholipids from phytophthora capsici mycelium

Comptes Rendus Biologies (1991)

V Pivot M. Bruneteau Peter Mas G. Michel

Phytophthora capsici

Isolation

Identification

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Citations (0)

ChemInform Abstract: STRUCTURE OF ITURINE C FROM BACILLUS SUBTILIS

Chemischer Informationsdienst (1978)

F. Peypoux F. Besson G. Michel L. Delcambe B.C. Das

Abstract Für den im Titel genannten Stoff Iturin Cwird anhand chemischer Reaktionen (saure Hydrolyse zu α‐ und βjAminosäuren; Diboran‐Reduktion), physikalischer Untersuchungen und Vergleich der MS‐Parameter der permethylierten Verbindung mit denen des bekannten perme‐ : thylierten Iturin Adie cyclische Struktur (I) ermittelt, die sowohl B‐Amino‐IZ‐methyltridecansäure als auch 3‐Amino‐l 2‐methyltetradecansäure enthält.

10.1002/chin.197834330

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Citations (1)

European Heart Journal Volume 20 (1999) Contents and European Heart Journal Supplements Volume 1 (1999) Contents

European Heart Journal (1999)

S Priori Jacques Barhanin Richard N.W. Hauer Wilhelm Haverkamp Habo J. Jongsma

Pharmacological treatment for

10.1053/euhj.1999.1953

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Citations (0)

Evolution du métabolisme des lécithines dans la membrane érythrocytaire au cours de la conservation du sang

Experientia (1971)

Maryvonne Ciavatti G. Michel

Blood conservation

10.1007/bf02136722

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Citations (4)

Interactions of antibiotics of the iturin group with human erythrocytes

Biochimica et Biophysica Acta (BBA) - Biomembranes (1986)

Chantal Latoud F. Peypoux G. Michel Roger Genet J.L. Morgat

Residue (chemistry)

10.1016/0005-2736(86)90144-6

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Citations (50)

Structure et activite biologique d'un sphingophospholipide isole de Phytophthora capsici

HAL (Le Centre pour la Communication Scientifique Directe) (1990)

M. Bruneteau Véronique Pivot Pierre Mas Paul-Michel Molot G. Michel

Phytophthora capsici

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Synthese du L‐alaninol a partir d'extraits acellulaires de Mycobacterium avium

FEBS Letters (1971)

M. Bruneteau G. Michel

A cell-free preparation was obtained from a culture of Mycobacterium avium. This preparation contained an L-alanine reductase which reduces L-alanine to L-alaninol, a constituant of the mycoside C(2). This reduction is better when ATP and NADH are present in the incubation medium.

Alanine

10.1016/0014-5793(71)80274-0

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Citations (3)

Composition of insect waxes. I. Waxes of exotic coccidae:Gascardia madagascariensis, Coccus ceriferus andTachardia lacca

Journal of the American Oil Chemists Society (1964)

E. Faurot‐Bouchet G. Michel

Abstract Composition of several coccid waxes has been determined by means of alumina and gas‐liquid chromatography. Coccus ceriferus wax is a mixture of the esters of C 26 and C 28 alcohols with C 24 , C 26 and C 28 acids. Tachardia lacca wax has a high percentage of free alcohols (essentially C 28 alcohol); Gascardia madagascariensis wax contains a large proportion of free acids. In addition to C 26 , C 32 and C 34 normal chain acids, there are several C 30 , C 32 and C 34 hydroxy acids, in which the hydroxyl function is situated in the middle of the hydrocarbon chain. Small proportions of odd and even hydrocarbons are present in all of the waxes investigated.

Long chain

10.1007/bf02654873

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Citations (24)

Proceedings: Androgen receptor in skeletal muscle.

PubMed (1975)

G. Michel E.-E. Baulieu

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Citations (4)

Overproduction and properties of the mannuronate alginate lyase AlxM_B

FEMS Microbiology Letters (1995)

Martine Malissard Frédéric Chavagnat Colette Duez Marie‐Jeanne Vacheron Micheline Guinand

In previous studies (Malissard et al., FEMS Microbiol. Lett. (1993) 110, 101-106), the alginate lyase AlxM of the marine bacterium ATCC 433367 was produced in Escherichia coli TC4/pAL-A3 with a yield of 50 micrograms per litre of culture. The polypeptide chain was cleaved between two cysteine residues, C169 and C183, themselves linked by a disulphide bridge. AlxM has now been overproduced in E. coli BL21(DE3)/pAL-Sur/pLysS. Under conditions in which formation of inclusion bodies can be avoided, the enzyme is synthesized as a catalytically active, water-soluble, unnicked polypeptide with a yield of 32 mg per litre of culture. It has been purified to protein homogeneity using a one-step procedure. The nicked AlxMA and unnicked AlxMB alginate lyases have identical alginate-degrading activities at high salt concentrations.

Inclusion bodies

Overproduction

10.1111/j.1574-6968.1995.tb07402.x

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Citations (12)