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1.
2.
Jean-Michel Panoff Bouachanh Thammavongs Jean-Marie Laplace Axel Hartke Philippe Boutibonnes Yanick Auffray 《Cryobiology》1995,32(6)
The physiology of the cold-shock response in Lactococcus lactis subsp. lactis IL1403 at a subzero temperature, and cold-induced adaptation to heat shock, were investigated. Preincubation of cells at 8°C led to the development of cryotolerance, i.e., an enhanced capacity to survive exposure to freezing temperature (-20°C). Pretreatment with chemicals considered to be chaotropic agents did not induce cryotolerance or, in contrast, led to a decrease in survival capacity at -20°C. Interestingly, preincubation at 8°C led also to thermololerance to a 52°C challenge, but preincubation of cells at 42°C for 30 min did not improve their capacity to survive freezing-thawing exposure. These results demonstrate that cold- and heat-shock responses are physiologically linked by a complex relation. Furthermore, food processing at low temperature before subzero or heat treatment may need to be reconsidered. 相似文献
3.
Summary Bacterial strains identified as Klebsiella pneumonia and Corynebacterium sp. degraded in few hours a great part of pure tara (Caesalpinia spinosa) tannin or crude water extract of tara pods powder. Large amounts of gallic acid were recovered during some experiments reaching 55 % of the theoretical yield in the best case. The feasibility of gallic acid production by a biotechnological process is discussed. 相似文献
4.
5.
Y Leclercq G Sawatzki J M Wieruszeski J Montreuil G Spik 《The Biochemical journal》1987,247(3):571-578
A 'serotransferrin-like' protein was purified from mouse milk. This serotransferrin cross-reacts immunologically with the serotransferrin isolated from mouse plasma and not with the mouse lactotransferrin (lactoferrin). Sugar analysis of the three transferrins, i.e. serotransferrin, milk 'serotransferrin-like' protein and lactotransferrin, revealed that the major difference between the glycan primary structure of mouse serotransferrin and those of mouse milk 'serotransferrin-like' protein and lactotransferrin concerns essentially the presence of one fucose residue in the last two proteins. For structural determination, the N-glycosidically linked glycans were released from the protein by a reductive cleavage of the oligosaccharide-protein linkage under strong alkaline conditions. The primary structure of the released oligosaccharide alditols was determined by methylation analysis and 400 MHz 1H-n.m.r. spectroscopy. The oligosaccharide alditols released from milk 'serotransferrin-like' protein and lactotransferrin were identical and were identified as disialylated biantennary glycans of the N-acetyl-lactosamine type with a fucose residue alpha-1,6-linked to the N-acetylglucosamine residue conjugated to the peptide chain and having the following primary structure: NeuAc(alpha 2-6)Gal(beta 1-4)GlcNAc(beta 1-2)Man(alpha 1-3)[NeuAc(alpha 2-6)Gal(beta 1-4)GlcNAc(beta 1-2)Man(alpha 1-6)]Man(beta 1-4)GlcNAc(beta 1-4)[Fuc(alpha 1-6)]GlcNAc(beta 1-N)Asn. The serotransferrin glycan has the same primary structure but is only partially fucosylated (10-15%). 相似文献
6.
Selection by Anion-Exchange Chromatography of Exopolysaccharide Mutants of the Cyanobacterium Synechocystis Strain PCC 6803
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The degree of retention of whole cells of Synechocystis strain PCC 6803 on DEAE-cellulose columns was shown to depend on their content of exopolysaccharides, which are at least in part responsible for the external negative charge of the cells. This feature was used for the isolation of mutants modified in the apparent viscosity caused by these macromolecular constituents. When a wild-type suspension was loaded onto a DE52 column, the cells eluting in the two extreme fractions of a 0 to 5 M NaCl step gradient represented 10−9 to 10−7 of the total eluted population. The accuracy of the procedure was established through the analysis of four clones: Suc(0)32 and Suc(0)65 (0 M) and Suc(5)64A and Suc(5)61 (5 M). The decreased viscosity of the exopolymers of the two 0 M clones, which appeared identical, could be related to the production of molecules less charged in uronic acids and more readily liberated from the cells. The two 5 M clones exhibited a lower sedimentation velocity, correlating with either a 60% increase in uronic acid and a doubling of the specific viscosity of the exopolysaccharides [clone Suc(5)64A] or a doubling of the per-cell production of polymers otherwise identical to those from wild-type cells [clone Suc(5)61]. 相似文献
7.
Gerard Strecker Jean-Michel Wieruszeski Jean-Claude Michalski Jean Montreuil 《Glycoconjugate journal》1988,5(4):385-396
The structure of a new nonasaccharide isolated from human milk has been investigated. By using methylation analysis, FAB-MS and1H-and13C-NMR spectroscopy as basic methods of structural investigation, this oligosaccharide was identified as VI2--Fuc,V4-Fuc,III3--Fuc-p-lacto-n-hexaose: Fuc1-2Gal1-3[Fuc1-4]GlcNAc1-3Gal1-4[Fuc1-3]GlcNAc1-3Gal1-4Glc.Abbreviations COSY
correlation spectroscope
- DP
degree of polymerisation
- FAB-MS
fast atom bombardment-mass spectrometry
- HPLC
high performance liquid chromatography
- NMR
nuclear magnetic resonance
- GLC
gas-liquid chromatography 相似文献
8.
Properties of the 12-O-Tetradecanoylphorbol-13-Acetate-Stimulated S6 Kinase from Rat Astroglial Cells 总被引:1,自引:0,他引:1
Danièle Toru-Delbauffe Jean-Michel Gavaret Claude Jacquemin Carole Matricon Martine Pomerance Michel Pierre 《Journal of neurochemistry》1988,51(5):1448-1454
The S6 kinase activity of astroglial cells in primary culture stimulated by 12-O-tetradecanoylphorbol-13-acetate (TPA) has been studied. This activity was eluted as a single peak at 0.15 M NaCl from a DEAE-Sephacel column. The chromatography of this peak on phosphocellulose revealed an activity eluted at 0.15 M NaCl. This partially purified enzyme had a sedimentation coefficient of 3.7S; Km values were 2 X 10(-5) M for ATP and 10(-6) M for 40S ribosomal subunits. The optimal Mg2+ concentration requirement was 2-3 mM. Mn2+ and Co2+ could substitute for Mg2+ (optimum concentrations 1.5 and 0.8 mM, respectively), but these cations were strong inhibitors in the presence of Mg2+. The enzyme was inhibited by N-ethylmaleimide, indicating that it contained thiol groups. This S6 kinase used ATP, but not GTP, as a phosphate donor, and exhibited great specificity for S6 as phosphate acceptor. Whole histones and protamine were slightly phosphorylated whereas phosvitin, histone H1, and surprisingly the peptide Arg-Arg-Leu-Ser-Ser-Leu-Arg-Ala were not phosphorylated. The TPA-stimulated S6 kinase resembles the insulin-, fibroblast growth factor- and cyclic AMP-stimulated enzymes, suggesting that several pathways might activate the same entity. 相似文献
9.
Henri Debray Danuta Dus Jean-Michel Wieruszeski Gérard Strecker Jean Montreuil 《Glycoconjugate journal》1991,8(1):29-37
Four bi-antennary glycan fractions of theN-acetyllactosamine-type, derived from a Lewis lung carcinoma (LL2) cell subline resistant to theAleuria aurantia agglutinin were studied by 400 MHz1H-NMR spectroscopy. By this method, their antennae were found to be terminated either by (2-3 or 6)-linkedN-acetylneuraminic acid or (1-3)-linked galactose residues. The primary structure of glycans of these four glycopeptide or derived oligosaccharide-alditols has been determined in full detail.Abbreviations NAc
N-acetyl group
- NGc
N-glycolyl group
- GlcNAc
N-acetylglucosamine
- NeuAc
N-acetylneuraminic acid
- NeuGc
N-glycolylneuraminic acid
- Man
mannose
- Gal
galactose
- Fuc
fucose
- Con A
concanavalin A
- LCA
Lens culinaris agglutinin
- AAA
Aleuria aurantia agglutinin
- WGA
Wheat germ agglutinin
- RCA II
Ricinus communis agglutinin II
- PBS
phosphate buffered saline, 0.01m Na2HPO4/0.14m NaCl, pH 7.2
- HPLC
high performance liquid chromatography
- EMEM
Eagle's Minimal Essential Medium
- LecR
lectin resistant
- MG
-methylglycoside 相似文献
10.
T Baussant G Strecker J M Wieruszeski J Montreuil J C Michalski 《European journal of biochemistry》1986,159(2):381-385
An endo-N-acetyl-beta-D-glucosaminidase active towards oligosaccharides with a reducing terminal [bis(N-acetylglucosamine)]residue has been characterized in rat liver. The primary structure of its reaction products was determined using high-resolution 1H-NMR spectroscopy. The enzyme is predominantly located in the lysosomal fraction, presents a maximum of activity at pH 3.5 and is completely inactive towards conjugated glycans, i.e. glycoproteins and glycopeptides as well as on glycoasparagines. These results support the existence of a new pathway for the degradation of glycoprotein glycans inside the lysosome. In particular, this enzymic activity may be the origin of oligosaccharides bearing a single terminal reducing N-acetylglucosamine residue which are excreted in the urine of patients with various exoglycosidase deficiencies. 相似文献