Search results for "Molecular mass"

showing 5 items of 155 documents

Cultivation ofZymomonas mobilis 113 S at Different Mixing Regimes and their Influence on the Levan Formation

2001

The Zymomonas mobilis I 13 S strain was cultivated in a bioreactor with a working volume of 1.4 I at different stirring regimes in a 15% initial sucrose medium The levan obtained in the fermentation process was analyzed by gel filtration. Because the sucrose/biomass ratio in the fermentation broth decreased to below 300 g/g, the insufficient concentration of sucrose might have decreased the concentration of levan. Besides the growth characteristics of the population, the mixing intensity and flow structure were also found to influence the molecular mass of levan. At 600 rpm, the microorganisms produced levan with a molecular mass lower than at 300 rpm. The stirring of a fermentation broth w…

education.field_of_studySucroseMolecular massbiologySize-exclusion chromatographyPopulationBioengineeringIndustrial fermentationequipment and suppliesbiology.organism_classificationApplied Microbiology and BiotechnologyZymomonas mobilischemistry.chemical_compoundchemistryBiochemistryBioreactorFermentationFood scienceeducationBiotechnologyActa Biotechnologica
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The shell matrix of the freshwater mussel Unio pictorum (Paleoheterodonta, Unionoida). Involvement of acidic polysaccharides from glycoproteins in na…

2007

13 pages; International audience; Among molluscs, the shell biomineralization process is controlled by a set of extracellular macromolecular components secreted by the calcifying mantle. In spite of several studies, these components are mainly known in bivalves from only few members of pteriomorph groups. In the present case, we investigated the biochemical properties of the aragonitic shell of the freshwater bivalve Unio pictorum (Paleoheterodonta, Unionoida). Analysis of the amino acid composition reveals a high amount of glycine, aspartate and alanine in the acid-soluble extract, whereas the acid-insoluble one is rich in alanine and glycine. Monosaccharidic analysis indicates that the in…

glycoproteinMESH: Amino AcidsMESH : PolysaccharidesMESH: BivalviaMESH : Calcification PhysiologicFresh WaterBiochemistryMESH : Spectroscopy Fourier Transform InfraredMESH : BivalviaSpectroscopy Fourier Transform InfraredMollusc shellMESH : Fresh Watercalcium-binding proteinElectrophoresis Gel Two-DimensionalMESH: AnimalsAmino Acidsmollusc shell nacreGel electrophoresisAlanine0303 health sciencesbiologyMESH : Carbohydrates030302 biochemistry & molecular biologyMESH : Extracellular Matrixmatrix macromoleculesExtracellular MatrixBiochemistryMESH: Fresh WaterElectrophoresis Polyacrylamide GelMESH: CarbohydratesFreshwater bivalveCarbohydratesMESH: GlycoproteinsMESH: Extracellular MatrixMESH : Electrophoresis Polyacrylamide GelMESH: Spectroscopy Fourier Transform InfraredMESH: Calcification Physiologic03 medical and health sciencesCalcification PhysiologicPolysaccharidesExtracellularAnimals[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsMolecular BiologyGlycoproteins030304 developmental biologyMolecular massUnio pictorumMESH : Electrophoresis Gel Two-DimensionalCell Biology[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/Biomaterialsbiology.organism_classificationbiomineralizationMESH: Electrophoresis Gel Two-DimensionalMESH : GlycoproteinsBivalviaIsoelectric pointMESH: PolysaccharidesMESH : Amino AcidsMESH : AnimalsMESH: Electrophoresis Polyacrylamide Gel
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Expression and characterization of the recombinant juvenile hormone epoxide hydrolase (JHEH) from Manduca sexta.

1998

The cDNA of the microsomal Juvenile Hormone Epoxide Hydrolase (JHEH) from Manduca sexta was expressed in vitro in the baculovirus system. In insect cell culture, the recombinant enzyme (Ms-JHEH) was produced at a high level (100 fold over background EH catalytic activity). As expected, Ms-JHEH was localized in the microsomal fraction with a molecular mass of approximately 50 kDa. Ms-JHEH showed a substrate and inhibitor spectrum similar to the wild type JHEH isolated from eggs of M. sexta. Its enzymatic activity was the highest for Juvenile Hormone III. Ms-JHEH hydrolyzed several trans-epoxides faster than cis-epoxides. A putative hydroxyl-acyl enzyme intermediate was isolated suggesting a …

mechanismGene ExpressionBiochemistryPolymerase Chain ReactionSubstrate SpecificityManduca sextaManducaHydrolaseAnimalsEpoxide hydrolaserecombinant enzymeMolecular BiologyDNA Primerschemistry.chemical_classificationEpoxide HydrolasesbiologyMolecular massBase Sequencejuvenile hormoneInsect cell cultureHydrogen-Ion Concentrationbiology.organism_classificationMolecular biologyRecombinant Proteinsepoxide hydrolaseJuvenile HormonesEnzymechemistryBiochemistryManduca sextaInsect ScienceJuvenile hormoneManducaBaculoviridaeInsect biochemistry and molecular biology
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Analysis of complement C3 activation products in human atherosclerotic lesions.

1991

Abstract Cleavage of the complement C3 protein is essential for complement activation. Saline extracts of human atherosclerotic lesions were examined by various techniques for the presence of C3 cleavage fragments. Crossed intermediate gel immunoelectrophoresis revealed that native C3 was the predominate C3 protein in extracts and that the C3dg fragment was also detected. SDS-PAGE/ Western blot analyses of lesion extracts employing monoclonal antibodies directed at C3c and C3dg fragment determinants demonstrated molecular weight bands corresponding to the known molecular weights of all the physiologic C3 cleavage fragments, except Cab which is known to have a short half-life. After C3, the …

medicine.diagnostic_testMolecular massArteriosclerosisBlotting WesternEnzyme-Linked Immunosorbent AssayImmunoelectrophoresisArteriesComplement C3BiologyCleavage (embryo)C3-convertasePeptide FragmentsComplement systemBlotBiochemistryWestern blotComplement C3bmedicineHumansLipid particleCardiology and Cardiovascular MedicineComplement ActivationImmunoelectrophoresisAtherosclerosis
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Analysis of liver-specific protein LSP using murine monoclonal antibodies.

1987

. We describe twenty murine monoclonal antibodies directed against different antigenic determinants of human and rabbit liver-specific protein LSP. Among them, nine were directed against liver-specific epitopes as judged from immunohistological studies. Immunoelectronmicroscopy revealed that seven of these monoclonals recognized membrane determinants differing in staining of distinct areas of the hepatocellular surface. Eleven antibodies were directed against intracellular structures. Western blot analysis showed that the epitopes detected were displayed on either single or multiple protein bands with apparent molecular weights between 24 000 and 60 000. Further differences were observed wi…

medicine.drug_classClinical BiochemistryMonoclonal antibodyBiochemistryEpitopeEpitopesMiceWestern blotAntigenmedicineAnimalsHumansbiologymedicine.diagnostic_testMolecular massAntibodies MonoclonalMembrane ProteinsProteinsGeneral MedicineMolecular biologyImmunohistochemistryStainingLiverAntigens Surfacebiology.proteinRabbitsAntibodyIntracellularEuropean journal of clinical investigation
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