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See detailEffets de la caséinase C et de l'iturine sur le virus grippal Lee
Rentier, Bernard ULg

Master's dissertation (1970)

Treating influenza B virus (Lee strain) by proteases caseinase C and iturin in a soft action provokes the "shaving" of surface projections ("spikes"). It modifies the sedimentation speed of the particles ... [more ▼]

Treating influenza B virus (Lee strain) by proteases caseinase C and iturin in a soft action provokes the "shaving" of surface projections ("spikes"). It modifies the sedimentation speed of the particles and allows for antigenic exploration of the envelope below the spikes. [less ▲]

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See detailIsolation of DD carboxypeptidase from Streptomyces albus G culture filtrates
Ghuysen, Jean-Marie ULg; Leyh-Bouille, Mélina; Bonaly, Roger et al

in Biochemistry (1970), 9(15), 2955-2961

Streptomyces albus G secretes a soluble DD carboxypeptidase whose catalytic activities are similar to those of the particulate DD carboxypeptidase from Escherichia coli. Both enzymes hydrolyze the C ... [more ▼]

Streptomyces albus G secretes a soluble DD carboxypeptidase whose catalytic activities are similar to those of the particulate DD carboxypeptidase from Escherichia coli. Both enzymes hydrolyze the C-terminal D-alanyl-D-alanine linkage of UDP-N-acetylmuramyl-L-alanyl-γ-D-glutamyl-(L)-meso-diaminopimelyl-(L)-D-alanyl-D-aIanine and the enzyme-peptide interactions have identical Michaelis constants. Like the E. coli enzyme, the Streptomyces DD carboxypeptidase exhibits endopeptidase activities. The Streptomyces enzyme is lytic for those walls in which the peptidoglycan interpeptide bonds are mediated through C-terminal D-alanyl-D linkages. There is no strict requirement for a specific structure of the C-terminal D-amino acid residue. The tripeptide Nα , Nє -bisacetyl-L-lysyl-D-alanyl-D-alanine is an excellent substrate for the Streptomyces DD carboxypeptidase. [less ▲]

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See detailStructure of the walls of Lactobacillus acidophilus strain 63 AM Gasser
Coyette, Jacques; Ghuysen, Jean-Marie ULg

in Biochemistry (1970), 9(15), 2935-2943

Peptidoglycan, neutral polysaccharide, and anionic polysaccharide are the main structural components of the walls of Lactobacillus acidophilus strain 63 AM Gasser. The peptide moiety of the peptidoglycan ... [more ▼]

Peptidoglycan, neutral polysaccharide, and anionic polysaccharide are the main structural components of the walls of Lactobacillus acidophilus strain 63 AM Gasser. The peptide moiety of the peptidoglycan is essentially composed of Nα-(L-alanyl-D-isoglutaminyl)-L-lysyl-D-alanine peptides, cross-linked by Nє-(D-alanyl-D-isoasparaginyl)-L-lysine bridges. The extent of peptide cross-linking is low. In log phase walls, the average size is of 2.3 cross-linked peptides, 10% of the peptide subunits occurring as monomers, 37% as dimers, and 30% as trimers. All of the peptide monomers and oligomers have D-alanyl-D-alanine sequences at their C termini, identified and measured with the help of a Streptomyces DD carboxypeptidase. The glycan moiety of the peptidoglycan is composed of β-1,4-N-acetylglucosaminyl-N-acetylmuramic acid units. All of the muramic acid residues are peptide substituted and about 60 to 70% of them have O-acetyl substituents on C6. The neutral polysaccharide is composed of equimolar amounts of glucose, galactose, and rhamnose. It is apparently linked to muramic acid residues of the peptidoglycan via phosphodiester groups. The extent of bridging is about 1 phosphate group for (glucose70-rhamnose70-galactose70) units. The anionic polysaccharide is a mixture of (a or β)-1,6-linked polyglucose polymers with monomeric α-glycerol phosphate side chains attached to them on C2 or C4 position. Peptidoglycan, neutral polysaccharide, and anionic polysaccharide represent 42, 32, and 17%, respectively, of the log-phase walls. Stationary-phase walls have similar composition and structure, except that substantial amounts of neutral polysaccharide are replaced by anionic polysaccharide. [less ▲]

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See detailLL-diaminopimelic acid containing peptidoglycans in walls of Streptomyces sp. and of Clostridium perfringens (type A).
Leyh-Bouille, Mélina; Bonaly, Roger; Ghuysen, Jean-Marie ULg et al

in Biochemistry (1970), 9(15), 2944-2952

In a major part of the wall peptidoglycans of Streptomyces sp. and of Clostridium perfringens, L-alanyl-D-isoglutaminyl-(L1)-LL-diaminopimelyl-(L1)-D-alanine peptides are cross-linked via D-alanylglycyl ... [more ▼]

In a major part of the wall peptidoglycans of Streptomyces sp. and of Clostridium perfringens, L-alanyl-D-isoglutaminyl-(L1)-LL-diaminopimelyl-(L1)-D-alanine peptides are cross-linked via D-alanylglycyl-(L2)-LL-diaminopimelic acid linkages (peptidoglycan of the chemotype II group). The Myxobacter AL-I endopeptidase hydrolyzes both D-alanyl-glycine and glycyl-LL-diaminopimelic acid linkages in the walls of C. perfringens, liberating free glycine. In contrast, the Myxobacter AL-I endopeptidase hydrolyzes only D-alanyl-glycine linkages in walls of Streptomyces sp. and the liberation of the glycine residues requires subsequent treatment with an aminopeptidase. No explanation for this observation can be proposed at this time. A minor component of the AL-I endopeptidase hydrolysate of the Streptomyces and C. perfringens walls is a resistant peptide dimer. Analyses indicate that the cross-link in this dimer may be mediated through LL-diamino-pimelylglycyl-LL-diaminopimelic acid linkages. The C termini of the peptide moieties in the wall peptidoglycans are either D-alanine or LL-diarninopimelic acid but never D-alanyl-D-alanine, thus indicating the presence in these microorganisms of carboxypeptidases similar to those of Escherichia coli. [less ▲]

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See detailSubstrate requirements of the Streptomyces albus G DD carboxypeptidase
Leyh-Bouille, Mélina; Ghuysen, Jean-Marie ULg; Bonaly, Roger et al

in Biochemistry (1970), 9(15), 2961-2970

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See detailOn the Streptomyces albus G DD carboxypeptidase mechanism of action of penicillin, vancomycin, and ristocetin
Leyh-Bouille, Mélina; Ghuysen, Jean-Marie ULg; Nieto, Manuel et al

in Biochemistry (1970), 9(15), 2971-2975

The activity of the D-alanyl-D carboxypeptidase from the penicillin-resistant Streptomyces albus G is not or very little affected by penicillins and related antibiotics. The molecular basis for the ... [more ▼]

The activity of the D-alanyl-D carboxypeptidase from the penicillin-resistant Streptomyces albus G is not or very little affected by penicillins and related antibiotics. The molecular basis for the mechanism of action of penicillin is discussed. The Streptomyces albus G D-alanyl-D carboxypeptidase appears as a model for the study of a mechanism of penicillin resistance that does not involve the enzymatic degradation of the antibiotic. Vancomycin and ristocetin are shown to inhibit the hydrolysis of sensitive peptides by the Streptomyces albus G D-alanyl-D carboxypeptidase and the mechanism of inhibition is discussed. [less ▲]

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See detailWall autolysin of Lactobacillus acidophilus strain 63 AM gasser
Coyette, Jacqueline; Ghuysen, Jean-Marie ULg

in Biochemistry (1970), 9(15), 2952-2955

The autolysin of Lactobacillus acidophilus strain 63 AM Gasser has the specificity of an endo-N-acetylmur-amidase. It hydrolyzes both N-acetylmuramic acid and N, O-diacetylmuramic acid linkages. It does ... [more ▼]

The autolysin of Lactobacillus acidophilus strain 63 AM Gasser has the specificity of an endo-N-acetylmur-amidase. It hydrolyzes both N-acetylmuramic acid and N, O-diacetylmuramic acid linkages. It does not exhibit any amidase or endopeptidase action. It is present in both log-phase and stationary-phase cells. In stationary-phase cells its action upon the wall peptido-glycan is inhibited. [less ▲]

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See detailDe la présence d'un glycopeptide dans la paroi de Bdello-vibrio vacteriovirus
Tinelli, Regina; Shilo, Moshe; Laurent, Maryvonne et al

in Comptes Rendus de l'Académie des Sciences. Série III, Sciences de la Vie (1970), 270

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See detailContribution to the study of the allosteric properties of acetylcholinesterase
Gridelet, J.; Foidart, Jean-Michel ULg; Wins, P.

in Archives Internationales de Physiologie et de Biochimie (1970), 78

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See detailInhibition of membrane-bound acetylcholinesterase by d-tubocurarine and its reversal by bivalent cations
Wins, P.; Schoffeniels, E.; Foidart, Jean-Michel ULg

in Life Sciences (1970), 9(5), 259-267

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See detailSymbiotic stars and related peculiar objects
Swings, Polydore ULg

in Spectroscopic astrophysics: an assessment of the contributions of Otto Struve (1970)

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See detailPossibility of Fluorescence Phenomena in the Ultraviolet Spectrum of Symbiotic Stars and Long Period Variables
Swings, Jean-Pierre ULg; Swings, Polydore ULg

in Houziaux, Léo; Butler, H. E. (Eds.) Ultraviolet Stellar Spectra and Related Ground-Based Observations : IAU symposium, held in Lunteren, The Netherlands, 24-27 June, 1969 (1970)

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See detailThe Evolution of a Peculiar Stellar Spectrum: Z Andromedae
Swings, Polydore ULg; Struve, Otto

in Herbig, G. H. (Ed.) Spectroscopic Astrophysics: An Assessment of the Contributions of Otto Struve (1970)

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See detailPhilosophie et politique de l'éducation
de Landsheere, Gilbert ULg

in Education : tribune libre d'information et de discussion pédagogiques (1970), (125), 53-58

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See detailEvolution récente de la distribution et shopping centers. En exemple le shopping center de Genk.
Merenne-Schoumaker, Bernadette ULg

in Bulletin de la Société Géographique de Liège (1970), (6), 91-119

Highlighting changes in the distribution (1960-1970) and more specific analysis of the "shopping centers " by studying the case of the Shopping center of Genk, the first having been opened in Belgium

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See detailActivité curarisante d'un Strychnos africain: le Strychnos usambarensis Gilg du Rwanda
Angenot, Luc ULg; Denoël, Albert; Goffart, Michel

in Journal de Pharmacie de Belgique (1970), 25(1), 73-77

The quaternary alkaloid fractions of the strychnos usambarensis root extract showed curarizing activity in frog and rat in vitro and in vivo.

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See detailVector analysis formulae.
Renson, Pierre ULg

in Bulletin de la Société Royale des Sciences de Liège (1970), 39

Not Available

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See detailEtude par spectrométrie de masse de l'Apparition des ions négatifs par Attachement Electronique Dissociatif dans des molécules polyatomiques.
Locht, Robert ULg

in Bulletin de l'Académie Royale des Sciences, des Lettres et des Beaux-Arts de Belgique. Sciences (1970), LVI(8), 788-817

The appearance of negative ions by dissociative electron attachment has been studied by electron impact on CH4, C2H2, C2H4 and C2H3X (X=F, Cl) using a sector field mass spectrometer. An interpretation has ... [more ▼]

The appearance of negative ions by dissociative electron attachment has been studied by electron impact on CH4, C2H2, C2H4 and C2H3X (X=F, Cl) using a sector field mass spectrometer. An interpretation has been attempted for the measured appearance potentials. The electronaffinity of C2 and C2H is found to be (3.3+/-0.3) eV and (2.3+/-0.2) eV respectively. Some evidence is brought for the existence of excited electronic states in polyatomic negative ions. [less ▲]

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