| dc.rights.license | CC0 | en_US |
| dc.rights.license | CC0 | en_US |
| dc.contributor.author | QUINTING, Birgit | |
| dc.contributor.author | Frère, Jean-Marie | |
| dc.contributor.author | Galleni, Moreno | |
| dc.contributor.author | Timm, Juliano | |
| dc.contributor.author | Gicquel, Brigitte | |
| dc.contributor.author | Amicosante, Gianfranco | |
| dc.date.accessioned | 2021-09-20T08:56:23Z | |
| dc.date.available | 2021-09-20T08:56:23Z | |
| dc.date.issued | 1997 | |
| dc.identifier.issn | 0378-1097 | en_US |
| dc.identifier.uri | https://luck.synhera.be/handle/123456789/1157 | |
| dc.identifier.doi | https://doi.org/10.1111/j.1574-6968.1997.tb10301.x | en_US |
| dc.description.abstract | p. 11-15 | en_US |
| dc.description.abstractfr | La β-lactamase de Mycobacterium smegmatis mc² 155 a été purifiée jusqu'à l'homogénéité des protéines. Sa séquence N-terminale et ses propriétés catalytiques sont similaires à celles de la β-lactamase produite par Mycobacterium fortuitum D316 et font de cette nouvelle enzyme un membre de la classe moléculaire A. | en_US |
| dc.description.abstracten | The β-lactamase of Mycobacterium smegmatis mc² 155 has been purified to protein homogeneity. Its N-terminal sequence and catalytic properties are similar to those of the β-lactamase produced by Mycobacterium fortuitum D316 and establish this new enzyme as a member of molecular class A. | en_US |
| dc.description.sponsorship | OTH | en_US |
| dc.description.sponsorship | OTH | en_US |
| dc.description.tableofcontents | 1 Introduction
2 Materials and methods
2.1 Antibiotics
2.2 Bacterial strains and culture conditions
2.3 Assay of protein concentration and enzyme activity
2.4 Purification of the β-lactamase
2.5 N-terminal amino acid sequence
2.6 Determination of kinetic parameters
2.7 Thermal stability and effects of chaotropic agents
2.8 Influence of the pH on the enzyme activity
3 Results and discussion
3.1 Production, purification, Mr and pI determinations
3.2 N-terminal amino acid sequence
3.3 Kinetic parameters
3.4 Thermal stability
3.5 Interaction of the enzyme with chaotropic agents
3.6 Influence of the pH on enzyme activity
4 Conclusion | en_US |
| dc.language.iso | EN | en_US |
| dc.publisher | Elsevier Science B.V. | en_US |
| dc.relation.ispartof | FEMS Microbiology Letters | en_US |
| dc.rights.uri | ? | en_US |
| dc.rights.uri | ? | en_US |
| dc.subject | Mycobacterium smegmatis | en_US |
| dc.subject | Mycobacterium smegmatis mc² 155 β-lactamase | en_US |
| dc.subject | purification | en_US |
| dc.title | Purification and properties of the Mycobacterium smegmatis mc² 155 β-lactamase | en_US |
| dc.title.fr | Purification et propriétés de la β-lactamase Mycobacterium smegmatis mc² 155 | en_US |
| dc.type | Article scientifique | en_US |
| synhera.classification | Sciences du vivant | en_US |
| synhera.classification | Sciences du vivant>>Microbiologie | en_US |
| synhera.institution | Autre | en_US |
| synhera.otherinstitution | Université de Liège, Centre d'Ingénierie des Protéines, Institut de Chimie, B6a | en_US |
| synhera.otherinstitution | Institut Pasteur (Paris), Unité de Génétique Mycobactérienne | en_US |
| synhera.otherinstitution | University of L'Aquila (Italie), Department of Science and Biomedical Technology and Biometrics, Institute of Biological Chemistry and Molecular Biology | en_US |
| synhera.stakeholders.fund | ? | en_US |
| synhera.stakeholders.fund | ? | en_US |
| synhera.cost.total | ? | en_US |
| synhera.cost.total | ? | en_US |
| synhera.cost.apc | ? | en_US |
| synhera.cost.apc | ? | en_US |
| synhera.cost.comp | ? | en_US |
| synhera.cost.comp | ? | en_US |
| synhera.cost.acccomp | ? | en_US |
| synhera.cost.acccomp | ? | en_US |
| dc.description.version | Oui | en_US |
| dc.rights.holder | ULiège | en_US |
| dc.rights.holder | ULiège | en_US |
