References of "Ghuysen, Jean-Marie"
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See detailAcetylhexosamine compounds enzymically released from Micrococcus lysodeikticus cell walls: III. The structure of di- and tetra-saccharides released from cell walls by lysozyme and Streptomyces F1 enzyme
Salton, M. R. J.; Ghuysen, Jean-Marie ULg

in Biochimica et Biophysica Acta (1960), 45

Two compounds, both of which have been isolated from cell walls of Micrococcus lysodeikticus digested with lysozyme or Streptomyces F1 enzyme, have been identified as di- and tetra-saccharides. The ... [more ▼]

Two compounds, both of which have been isolated from cell walls of Micrococcus lysodeikticus digested with lysozyme or Streptomyces F1 enzyme, have been identified as di- and tetra-saccharides. The reducing groups of the di- and tetra-saccharides and those of the high-molecular weight, non-dialysable compounds belong to muramic acid. [beta]-glucosidase yields free N-acetylglucosamine and N-acetylmuramic acid from the di- and tetra-saccharides. The proposed structure for the di-saccharide liberated by lysozyme and F1 is: 6-O-[beta]-N-acetylglucosaminyl-N-acetylmuramic acid. The tetra-saccharides isolated from lysozyme and F1 digests appear to be identical. The structure proposed for the tetra-saccharide isolated from lysozyme digested walls is: O-[beta]-N-acetylglucosaminyl-(I-->6)-O-[beta]-N-acetylmuraminyl-(I-->4)-O-[beta]-N-acetylglucosaminyl- (I-->6)-[beta]-N-acetylmuramic acid. Both lysozyme and Streptomyces F1 enzyme degrade di- and tetra-chitobiose, indicating their [beta](I-->4) N-acetyl hexosaminidase activity. [less ▲]

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See detailAcetylhexosamine compounds enzymically released from micrococcus lysodeikticus cell walls: II. Enzymic sensitivity of purified acetylhexosamine and acetylhexosamine-peptide complexes
Ghuysen, Jean-Marie ULg

in Biochimica et Biophysica Acta (1960), 40

Free di-saccharide (N-acetylglucosamine-N-acetylmuramic acid) is released from a purified amino sugar complex, probably tetra-saccharide, by the action of egg-white lysozyme and of a similar enzyme ... [more ▼]

Free di-saccharide (N-acetylglucosamine-N-acetylmuramic acid) is released from a purified amino sugar complex, probably tetra-saccharide, by the action of egg-white lysozyme and of a similar enzyme secreted by a Streptomyces. The di-saccharide is also released from a purified poly-acetylamino sugar-peptide-di-saccharide compound by the action of the same enzymes on its poly-acetylamino sugar moiety. Differences in the affinity of egg-white lysozyme and of the Streptomyces enzyme for their substrates are discussed. A second bacteriolytic enzyme, also secreted by the Streptomyces, liberates free disaccharide from the purified peptide-di-saccharide and poly-acetylamino sugar-peptide-di-saccharide complexes by splitting the bond between the carboxyl group of muramic acid and the amino group of the peptide moiety. [less ▲]

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See detailAcetylhexosamine compounds enzymically released from Micrococcus lysodeikticus cell walls: I. Isolation and composition of acetylhexosamine and acetylhexosamine-peptide complexes
Ghuysen, Jean-Marie ULg; Salton, M. R. J.

in Biochimica et Biophysica Acta (1960), 40

Some of the dialyzable products of the digestion of Micrococcus lysodeikticus cell walls by lysozyme and by a similar enzyme secreted by a Streptomyces have been isolated and their compositions determined ... [more ▼]

Some of the dialyzable products of the digestion of Micrococcus lysodeikticus cell walls by lysozyme and by a similar enzyme secreted by a Streptomyces have been isolated and their compositions determined. The two simplest substances released by both enzymes are (a) a di-saccharide of N-acetylmuramic acid-N-acetylglucosamine and (b) an N-acetylmuramic acid-N-acetylglucosamine complex. Seven peptide-acetyl-amino sugar complexes have been isolated. All seven compounds contain lysine, glutamic acid, glycine, alanine in the same molecular proportions as found in the original cell wall and a di-saccharide moiety of N-acetylmuramic acid and N-acetylglucosamine. One of the peptide-amino sugar complexes contains in addition a polysaccharide moiety [N-acetylmuramic acid-N-acetylglucosamine]10. [less ▲]

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See detailLe carbamate de propynylcyclohexanol étude pharmacologique et biologique
Charlier, R.; Prost, M.; Dierickx, L. et al

in Archives Internationales de Pharmacodynamie et de Thérapie (1959), 119(1-2), 264-274

Propnylcyclohexanol carbamate (L.2103) has more intense hypnotic and sedative properties, and a better therapeutic index than the carbamates of homologous propargylic cycloaliphatic carbinols. The synergy ... [more ▼]

Propnylcyclohexanol carbamate (L.2103) has more intense hypnotic and sedative properties, and a better therapeutic index than the carbamates of homologous propargylic cycloaliphatic carbinols. The synergy between L.2103 and chlorpromazine, barbiturates, and the promethazine-pethidine association is demonstrated, as well as the antagonism of L.2103 in regard to some convulsant drugs acting at various levels of the central nervous system. Although having sedative properties, L.2103 administered by oral and parental routes to the dog, has been studied. The percentage of reducing metabolites found in the urines is small and persists longer than hypnotic activity. The nature of these metabolites is discussed. [less ▲]

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See detailEffet de la mescaline, du lsd 25 et de dérivés de l'adrenochrome sur la décarboxlyase glutamique du cerveau
Deltour, G. H.; Ghuysen, Jean-Marie ULg; Claus, A.

in Biochemical Pharmacology (1959), 1(4), 267-272

The inhibitory effect of adrenochrome on glutamic decarboxylase from brain homogenates in vitro, does not occur with mescaline and LSD 25. Certain stable derivatives of adrenochrome such as MSCA and AHA ... [more ▼]

The inhibitory effect of adrenochrome on glutamic decarboxylase from brain homogenates in vitro, does not occur with mescaline and LSD 25. Certain stable derivatives of adrenochrome such as MSCA and AHA, in which the quinonic function is blocked, have an opposite effect, and behave like activators of brain glutamic decarboxylase. This activation seems to be indirect; MSCA and AHA do not constitute new coenzymes. [less ▲]

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See detailLes activités antimicrobiennes des détergents
Ghuysen, Jean-Marie ULg

in Revue Médicale de Liège (1957), 12(17), 457-464

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See detailActivités bacteriolytiques de l'actinomycetine de Streptomyces albus G.
Ghuysen, Jean-Marie ULg

in Archives Internationales de Physiologie et de Biochimie (1957), 65(2), 173-305

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See detailActivités bactériolytiques de l’actinomycétine de streptomyces albus G
Ghuysen, Jean-Marie ULg

Post doctoral thesis (1957)

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See detailAction de l'actinomycetine sur les parois cellulaires bacteriennes
Salton, M. R. J.; Ghuysen, Jean-Marie ULg

in Biochimica et Biophysica Acta (1957), 24(1), 160-173

The cell walls of a number of gram-positive bacteria can be digested by two different enzymes, present in actinomycetin, which have been obtained in a purified form. In contrast to lysozyme and the ... [more ▼]

The cell walls of a number of gram-positive bacteria can be digested by two different enzymes, present in actinomycetin, which have been obtained in a purified form. In contrast to lysozyme and the streptolytic enzyme of McCarty, these two enzymes are peptidases, their lytic action on the cell walls being accompanied by the liberation of alanine and/or glycine and small dialysable peptides. The ionic strength of the medium plays an essential role in the lysis. This role has been described and it probably depends on the electric charge of the cell walls. The products of the digestion of cell walls of staphylococci have been specially studied: at least some of the liberated alanine has the D-form; the non-dialysable fractions have been examined by electrophoresis and by ultra-centrifugation. [less ▲]

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See detailAction de l'actinomycetine sur le fibrinogene et la fibrine.
Ghuysen, Jean-Marie ULg; Welsh, Maurice

in Comptes Rendus des Séances de la Société de Biologie et de ses Filiales (1954), 148(19-20), 1694-1697

Actinomycetin rapidly digests freshly formed (unretracted) fibrin. The keratinolytic principle is capable of digesting retracted fibrin obtained by whipping the clot.

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See detailConcentration et purification des principes bacteriolytiques de l'actinomycetine par chromatographie sur corps microbiens.
Ghuysen, Jean-Marie ULg; Welsch, Maurice

in Comptes Rendus des Séances de la Société de Biologie et de ses Filiales (1954), 148(13-14), 1283-1287

En introduisant d'épaisses suspensions microbiennes dans une quantité donnée d'actinomycétine (1*), maintenue à 2° pour éviter la bactériolyse, nous avons montré que les principes colilytique et ... [more ▼]

En introduisant d'épaisses suspensions microbiennes dans une quantité donnée d'actinomycétine (1*), maintenue à 2° pour éviter la bactériolyse, nous avons montré que les principes colilytique et staphylotytique (2*à 6*) peuvent être adsorbés sur les corps microbiens (7*). Escherichia coli et Micrococcus pyogenes aureus adsorbent, l'un et l'autre, ces deux agents lytiques ; mais leur capacité d'adsorption est toujours plus grande pour le principe homologue. L'adsorption est particulièrement efficace si elle est réalisée à un pH voisin de 9 et à force ionique faible. L'élution, réalisable ensuite par solution saline, permet d'obtenir les principes lytiques concentrés et, dans une certaine mesure, purifiés. Dans la présente note, le mécanisme de cette adsorption est étudié de façon plus précise, en utilisant une technique analogue à celle de la chromatographie. (1*) M. Welsch, C. R. Soc. Biol., 1937. t. 126, p. 244 : J. Bacter., 1947, t. 53, p. 101 ; Rev. belge pathol. Méd. expérim., 1947, t. 18, suppl. 2. [less ▲]

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See detailL'activité antibiotique du type actinomycetine chez les Streptomyces
Ghuysen, Jean-Marie ULg; Leger, G.; Welsch, Maurice

in Comptes Rendus des Séances de la Société de Biologie et de ses Filiales (1954), 148(19-20), 1691-1693

cf. C.A. 47, 6491c; 49, 422d. Actinomycetin, obtained from Streptomyces albus G, was shown to contain 5 distinct enzymes which attack, resp., heat-killed Escherichia coli, keratin, mucin, casein, and a ... [more ▼]

cf. C.A. 47, 6491c; 49, 422d. Actinomycetin, obtained from Streptomyces albus G, was shown to contain 5 distinct enzymes which attack, resp., heat-killed Escherichia coli, keratin, mucin, casein, and a component of the epidermis the destruction of which results in epidermal desquamation and loosening of the hair. The substrate of this last enzyme is a complex protein component of the skin extractable by urea soln. (with or without KCl) at 25°. Another fraction of the epidermis, extractable under similar conditions at 0°, appears to be sensitive to the keratinolytic enzyme. [on SciFinder(R)] [less ▲]

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See detailActivite pneumolytique de l'actinomycetine.
Ghuysen, Jean-Marie ULg; Welsch, Maurice

in Comptes Rendus des Séances de la Société de Biologie et de ses Filiales (1954), 148(7-8), 729-732

The actinomycetin of the culture filtrate of Streptomyces albus G is a mixt. of at least 4 different agents which play a part in the lysis of live or heat-killed pneumococci. Two are identical with lytic ... [more ▼]

The actinomycetin of the culture filtrate of Streptomyces albus G is a mixt. of at least 4 different agents which play a part in the lysis of live or heat-killed pneumococci. Two are identical with lytic agents previously shown to act on other micro.ovrddot.organisms, and two appear to be specific for pneumococci. [on SciFinder(R)] [less ▲]

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See detailL'activité antibiotique du type actinomycetine chez les Streptomyces.
Bergamini, Lucia; Ghuysen, Jean-Marie ULg; Welsch, Maurice

in Comptes Rendus des Séances de la Société de Biologie et de ses Filiales (1954), 148(7-8), 733-736

The various enzymic and bacteriolyric activities found in the actinomycetin of Streptomyces albus are frequently found, more or less assocd., in actinomycetins from other species of Streptomyces. The ... [more ▼]

The various enzymic and bacteriolyric activities found in the actinomycetin of Streptomyces albus are frequently found, more or less assocd., in actinomycetins from other species of Streptomyces. The different activities are exerted by different agents present in variable proportion in the prepns. These agents can be sepd. [on SciFinder(R)] [less ▲]

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See detailInfluence des ions bivalents et de la témperature sur la production et les activités des principes bacteriolytiques de l'actinomycetine
Ghuysen, Jean-Marie ULg; Welsch, Maurice

in Comptes Rendus des Séances de la Société de Biologie et de ses Filiales (1953), 147(15-18), 1502-1505

L'actinomycétine (1*), filtrat de culture bactériolytique de certains Streptomyces, provoque la dissolution des bactéries tuées d'une part de certains microorganismes gram-positifs vivants d'autre part (2 ... [more ▼]

L'actinomycétine (1*), filtrat de culture bactériolytique de certains Streptomyces, provoque la dissolution des bactéries tuées d'une part de certains microorganismes gram-positifs vivants d'autre part (2*). Ces deux activités sont attribuables, au moins en partie, à des agents distincts (3*, 4*, 5*, 6*), que nous pouvons désigner commodément sous les noms respectifs de : principe colilytique et principe staphylolytique. Nous montrons, dans cette note, que la présence de cations bivalents, dans le milieu de culture où l'actinomycétine est élaborée, modifie le rendement en principes lytiques et la cinétique de leur activité. (1*) M. Welsch, C. R. de la Soc. de Biol., 1937, t. 126, p. 244 ; J. Bacter., 1947, t. 53, p. 101. (2*) M. Welsch, Reυ. belge Pathol. Méd. expérim., 1947, t. 18, suppl. 2. (3*) M. Welsch, Bull. Soc. Chim. biol, 1947, t. 29, p. 362. (4*) J. M. Ghuysen, C. R. de. la Soc. de Biol., 1952, t. 146, p. 1268. (5*) J. M. Ghuysen, C. R. de la Soc. de Biol., 1952, t. 146, p. 1812. (6*) J. M. Ghuysen, Arch. intern. Physiol., 1953, t. 61, p. 259. [less ▲]

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See detailDualité des principes bactériolytiques de l'actinomycetine.
Ghuysen, Jean-Marie ULg

in Archives Internationales de Physiologie (1953), 61(2), 259-260

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See detailActivité streptolytique de l'actinomycetine
Welsch, Maurice; Ghuysen, Jean-Marie ULg

in Comptes Rendus des Séances de la Société de Biologie et de ses Filiales (1953), 147(19-20), 1659-1662

Partially purified actinomycetin contains, in addn. to the colilytic and staphylolytic principles previously reported, an agent which lyses streptococci. [on SciFinder(R)]

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See detailAnalyse et purification de l'actinomycetine par absorption
Ghuysen, Jean-Marie ULg; Welsch, Maurice

in Comptes Rendus des Séances de la Société de Biologie et de ses Filiales (1952), 146(21-22), 1812-1815

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See detailL'activité staphylolytique de l'actinomycétine
Ghuysen, Jean-Marie ULg

in Comptes Rendus des Séances de la Société de Biologie et de ses Filiales (1952), 146(15-16), 1268-1271

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