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Titre : Purification et caractérisation des lectines à partir des champignons : Lactarius deliciosus, Laetiporus sulphureus avec des tests biologiques. Type de document : texte imprimé Auteurs : Mohammed Esseddik Toumi, Auteur ; Youcef Necib, Directeur de thèse Mention d'édition : 22-sept-21 Editeur : جامعة الإخوة منتوري قسنطينة Année de publication : 2021 Importance : 123 f. Format : 30 cm. Note générale : Doctorat 3éme CYCLE LMD.
1 copies imprimées disponibles
Langues : Français (fre) Catégories : Français - Anglais
BiologieTags : Biochimie et Biologie Cellulaire et Moléculaire: Biochimie Appliquée lectine Lactarius deliciosus agglutination affinité spécifique clairance activité phagocytaire Laetiporus sulphureus, MALDI-TOF/TOF, activité cytotoxique Lactarius Deliciosus Lectine خاصية الارتباط جاذبية تصريح نشاط بلعمي MALDI-TOF /TOF Laetiporus Sulphureus نشاط سمي خلاوي Index. décimale : 570 Sciences de la vie. Biologie Résumé :
In this study, two fungal lectins having a lactose affinity have been purified and characterized from Lactarius deliciosus strain TME25 and Laetiporus sulphureus strain TME43 (called LDL and PSLec respectively) by different chromatographic techniques and its biological potentials were evaluated. The characterization of LDL showed that it is a heterodimeric haemagglutinin (18 and 19 kDa molecular weight for each unit), specific for galactose and methyl-α-d-galactopyranoside; affinity for lactose, fetuin and Mucin. LDL induces agglutination (ha) at temperatures below 70 ° C, and in optimal pH equal to 7. The immunomodulation assay (carbon clearance test) by LDL in vivo showed a highly significant effect of phagocyte activity of mice reticulo-endothelial system at p <0.0001. The PSLec was characterized by a homotetrameric structure of 35,904 kDa of each subunits determined by LC-MS/MS-MALDI. It is a metallodependent lectin, stable at alkali pH. In addition, the proteomic study of the mask of these peptides fragmented by the trypsin and MALDI-TOF/TOF showed us that PSLec has an identity score of 43 with the Autophagy-related protein 16 from Meyerozyma guilliermondii (ATCC strain 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y -324) (Expasy Id: ATG16_PICGU). The antimtimoral preliminary assay MTT revealed that PSLec is a cytotoxic lectin.
Note de contenu :
Annexes.Diplôme : Doctorat En ligne : ../theses/biologie/TOU7799.pdf Format de la ressource électronique : Permalink : https://bu.umc.edu.dz/md/index.php?lvl=notice_display&id=11631 Purification et caractérisation des lectines à partir des champignons : Lactarius deliciosus, Laetiporus sulphureus avec des tests biologiques. [texte imprimé] / Mohammed Esseddik Toumi, Auteur ; Youcef Necib, Directeur de thèse . - 22-sept-21 . - جامعة الإخوة منتوري قسنطينة, 2021 . - 123 f. ; 30 cm.
Doctorat 3éme CYCLE LMD.
1 copies imprimées disponibles
Langues : Français (fre)
Catégories : Français - Anglais
BiologieTags : Biochimie et Biologie Cellulaire et Moléculaire: Biochimie Appliquée lectine Lactarius deliciosus agglutination affinité spécifique clairance activité phagocytaire Laetiporus sulphureus, MALDI-TOF/TOF, activité cytotoxique Lactarius Deliciosus Lectine خاصية الارتباط جاذبية تصريح نشاط بلعمي MALDI-TOF /TOF Laetiporus Sulphureus نشاط سمي خلاوي Index. décimale : 570 Sciences de la vie. Biologie Résumé :
In this study, two fungal lectins having a lactose affinity have been purified and characterized from Lactarius deliciosus strain TME25 and Laetiporus sulphureus strain TME43 (called LDL and PSLec respectively) by different chromatographic techniques and its biological potentials were evaluated. The characterization of LDL showed that it is a heterodimeric haemagglutinin (18 and 19 kDa molecular weight for each unit), specific for galactose and methyl-α-d-galactopyranoside; affinity for lactose, fetuin and Mucin. LDL induces agglutination (ha) at temperatures below 70 ° C, and in optimal pH equal to 7. The immunomodulation assay (carbon clearance test) by LDL in vivo showed a highly significant effect of phagocyte activity of mice reticulo-endothelial system at p <0.0001. The PSLec was characterized by a homotetrameric structure of 35,904 kDa of each subunits determined by LC-MS/MS-MALDI. It is a metallodependent lectin, stable at alkali pH. In addition, the proteomic study of the mask of these peptides fragmented by the trypsin and MALDI-TOF/TOF showed us that PSLec has an identity score of 43 with the Autophagy-related protein 16 from Meyerozyma guilliermondii (ATCC strain 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y -324) (Expasy Id: ATG16_PICGU). The antimtimoral preliminary assay MTT revealed that PSLec is a cytotoxic lectin.
Note de contenu :
Annexes.Diplôme : Doctorat En ligne : ../theses/biologie/TOU7799.pdf Format de la ressource électronique : Permalink : https://bu.umc.edu.dz/md/index.php?lvl=notice_display&id=11631 Exemplaires (1)
Code-barres Cote Support Localisation Section Disponibilité TOU/7799 TOU/7799 Thèse Bibliothèque principale Thèses Disponible Extraction, purification, caractérisation et effet immuno-modulateur Des lectines fongiques de Terfèzia boudiéri (Truffe Blanche du Sahara) / Abdelbaki Zitouni
Titre : Extraction, purification, caractérisation et effet immuno-modulateur Des lectines fongiques de Terfèzia boudiéri (Truffe Blanche du Sahara) Type de document : texte imprimé Auteurs : Abdelbaki Zitouni, Auteur ; Youcef Necib, Directeur de thèse Editeur : جامعة الإخوة منتوري قسنطينة Année de publication : 2015 Importance : 140 f. Format : 30 cm. Note générale : 2 copies imprimées disponibles
Langues : Français (fre) Catégories : Français - Anglais
BiologieTags : Lectines Extraction Purification Agglutination Activité phagocytaire Lectins Activity Phagocytic Cells استخلاص تنقية اللكتينات تراص نشاط الخلايا البالعة Index. décimale : 570 Sciences de la vie. Biologie Résumé : Lectins are ubiquitous, polyvalent and non immune origin which bind specifically and reversibly to carbohydrates. They are often multivalent and have the well-known ability to agglutinate erythrocytes.
Fungi, including microscopic fungi and yeasts, have been the subject of considerable interest in recent years because of their potential biomedical and biotechnological applications. The information on fungal lectins, especially the structural point of view, are minimal compared to those of their plant and animal counterparts. It is in this context that lies our purpose was realized by the biochemical and structural characterization of fungal lectin Terfezia boudieri ( Algerian Sahara Truffle) on which we previously had no such data.
Two lectins: TrFBL1 and TrFBL2 were extracted, purified, characterized and sequened. The structures of 3D TrFBL1 native protein and its complex with a ligand, fucoside sélénométhyl were obtained and are being refined .The structures of TrFBL2 complexes with N-acetylglucosamine and two other glycans were obtained at high resolution.
The Genome of Terfezia boudieri was obtained and is available from the month of December 2013 and will become part of the database collected Lectin 3D (http://lectin3d.cermav.cnrs.fr).
Diplôme : Doctorat en sciences En ligne : ../theses/biologie/ZIT6699.pdf Format de la ressource électronique : Permalink : https://bu.umc.edu.dz/md/index.php?lvl=notice_display&id=9924 Extraction, purification, caractérisation et effet immuno-modulateur Des lectines fongiques de Terfèzia boudiéri (Truffe Blanche du Sahara) [texte imprimé] / Abdelbaki Zitouni, Auteur ; Youcef Necib, Directeur de thèse . - جامعة الإخوة منتوري قسنطينة, 2015 . - 140 f. ; 30 cm.
2 copies imprimées disponibles
Langues : Français (fre)
Catégories : Français - Anglais
BiologieTags : Lectines Extraction Purification Agglutination Activité phagocytaire Lectins Activity Phagocytic Cells استخلاص تنقية اللكتينات تراص نشاط الخلايا البالعة Index. décimale : 570 Sciences de la vie. Biologie Résumé : Lectins are ubiquitous, polyvalent and non immune origin which bind specifically and reversibly to carbohydrates. They are often multivalent and have the well-known ability to agglutinate erythrocytes.
Fungi, including microscopic fungi and yeasts, have been the subject of considerable interest in recent years because of their potential biomedical and biotechnological applications. The information on fungal lectins, especially the structural point of view, are minimal compared to those of their plant and animal counterparts. It is in this context that lies our purpose was realized by the biochemical and structural characterization of fungal lectin Terfezia boudieri ( Algerian Sahara Truffle) on which we previously had no such data.
Two lectins: TrFBL1 and TrFBL2 were extracted, purified, characterized and sequened. The structures of 3D TrFBL1 native protein and its complex with a ligand, fucoside sélénométhyl were obtained and are being refined .The structures of TrFBL2 complexes with N-acetylglucosamine and two other glycans were obtained at high resolution.
The Genome of Terfezia boudieri was obtained and is available from the month of December 2013 and will become part of the database collected Lectin 3D (http://lectin3d.cermav.cnrs.fr).
Diplôme : Doctorat en sciences En ligne : ../theses/biologie/ZIT6699.pdf Format de la ressource électronique : Permalink : https://bu.umc.edu.dz/md/index.php?lvl=notice_display&id=9924 Exemplaires (1)
Code-barres Cote Support Localisation Section Disponibilité ZIT/6699 ZIT/6699 Thèse Bibliothèque principale Thèses Disponible
