Search results for "Amide"

showing 10 items of 3119 documents

Chlorophyll-Protein Complexes of Chlorella fusca

1980

Chlorophyll-protein complexes from thylakoids of the normal type and two mutants of Chlorella fusca were separated using sodium dodecyl sulfate acrylamide gel electrophoresis (PAGE). The properties of the chlorophyll-protein complexes of the three strains of Chlorella were compared. Standard curves were set up for the characterization of the chlorophyll-proteins. In every electrophoretic separation of chlorophyll-protein complexes, a certain amount of pigment is separated from the protein. We tried to keep that amount as low as possible by mild solubiliza­tion and by working in low temperature. Under these conditions, we obtained several new chlorophyll-proteins in addition to the P-700-chl…

Chlorophyll bPhotosynthetic reaction centreChlorophyll abiologyPhotosystem Ibiology.organism_classificationGeneral Biochemistry Genetics and Molecular Biologychemistry.chemical_compoundChlorellachemistryChlorophyllSodium dodecyl sulfatePolyacrylamide gel electrophoresisNuclear chemistryZeitschrift für Naturforschung C
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The negatively charged amino acids in the lumenal loop influence the pigment binding and conformation of the major light-harvesting chlorophyll a/b c…

2008

AbstractThe major chlorophyll (Chl) a/b complexes of photosystem II (LHCIIb), in addition to their primary light-harvesting function, play key roles in the organization of the granal ultrastructure of the thylakoid membranes and in various regulatory processes. These functions depend on the structural stability and flexibility of the complexes. The lumenal side of LHCIIb is exposed to broadly variable pH environments, due to the build-up and decay of the pH gradient during photosynthesis. Therefore, the negatively charged amino acids in the lumenal loop might be of paramount importance for adjusting the structure and functions of LHCIIb. In order to clarify the structural roles of these res…

ChlorophyllCircular dichroismPhotosystem IIPigment bindingMolecular ConformationBiophysicsPhotosynthesisBiochemistryMajor light-harvesting a/b complex of photosystem IILow pHAmino AcidsSpectroscopyPhotosystemchemistry.chemical_classificationChemistryCircular DichroismPhotosystem II Protein ComplexPigments BiologicalCell BiologyHydrogen-Ion ConcentrationAmino acidCrystallographyB vitaminsMutagenesisThylakoidBiophysicsElectrophoresis Polyacrylamide GelProtein BindingBiochimica et Biophysica Acta (BBA) - Bioenergetics
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Carotenoid binding sites in LHCIIb

2000

The major light-harvesting complex of photosystem II can be reconstituted in vitro from its bacterially expressed apoprotein with chlorophylls a and b and neoxanthin, violaxanthin, lutein, or zeaxanthin as the only xanthophyll. Reconstitution of these one-carotenoid complexes requires low-stringency conditions during complex formation and isolation. Neoxanthin complexes (containing 30–50% of the all-trans isomer) disintegrate during electrophoresis, exhibit a largely reduced resistance against proteolytic attack; in addition, energy transfer from Chl b to Chl a is easily disrupted at elevated temperature. Complexes reconstituted in the presence of either zeaxanthin or lutein contain nearly …

ChlorophyllLuteinPhotosynthetic Reaction Center Complex ProteinsPigment bindingLight-Harvesting Protein ComplexesXanthophyllsBiologyBinding CompetitiveBiochemistrySubstrate SpecificityLight-harvesting complexchemistry.chemical_compoundNeoxanthinZeaxanthinsTrypsinProtein PrecursorsCarotenoidPlant Proteinschemistry.chemical_classificationBinding SitesChlorophyll ALuteinPhotosystem II Protein Complexfood and beveragesPigments BiologicalPlantsbeta CaroteneCarotenoidseye diseasesZeaxanthinEnergy TransferchemistryBiochemistryXanthophyllElectrophoresis Polyacrylamide GelApoproteinsViolaxanthinEuropean Journal of Biochemistry
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The Folding State of the Lumenal Loop Determines the Thermal Stability of Light-Harvesting Chlorophyll a/b Protein

2004

The major light-harvesting protein of photosystem II (LHCIIb) is the most abundant chlorophyll-binding protein in the thylakoid membrane. It contains three membrane-spanning alpha helices; the first and third one closely interact with each other to form a super helix, and all three helices bind most of the pigment cofactors. The protein loop domains connecting the alpha helices also play an important role in stabilizing the LHCIIb structure. Single amino acid exchanges in either loop were found to be sufficient to significantly destabilize the complex assembled in vitro [Heinemann, B., and Paulsen, H. (1999) Biochemistry 38, 14088-14093. Mick, V., Eggert, K., Heinemann, B., Geister, S., and…

ChlorophyllProtein DenaturationProtein FoldingPhotosystem IILight-Harvesting Protein ComplexesBiochemistryProtein structureTrypsinPlant Proteinschemistry.chemical_classificationChemistryChlorophyll AHydrolysisPeasTemperaturePhotosystem II Protein ComplexSodium Dodecyl SulfateProtein Structure TertiaryAmino acidKineticsCrystallographyAmino Acid SubstitutionMembrane proteinThylakoidHelixBiophysicsElectrophoresis Polyacrylamide GelProtein foldingAlpha helixBiochemistry
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Displacement of phenprocoumon (Marcumar) from albumin by sulfonylurea compounds, suramin, and ioglycamic acid.

1972

The technique of Sephadex gel filtration was employed to characterize the effect of some sulfonylurea compounds, ioglycamic acid, and suramin on the binding of phenprocoumon to bovine serum albumin.

ChlorpropamideChlorpropamideSuraminTolbutamideSerum albuminSuraminIn Vitro TechniquesBenzoatesPhenprocoumonCoumarinsBenzyl CompoundsmedicineAnimalsBovine serum albuminPharmacologyChromatographyBinding SitesbiologyChemistryAlbuminAnticoagulantsDextransSerum Albumin BovineGeneral MedicineCarbutamideGlycolatesCarbutamideSulfonylurea CompoundsSephadexbiology.proteinChromatography GelIodobenzoatesCattlemedicine.drugProtein BindingNaunyn-Schmiedeberg's archives of pharmacology
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CLINICAL AND EXPERIMENTAL STUDIES WITH CHLORPROPAMIDE IN DIABETES MELLITUS, IN NORMAL INDIVIDUALS, AND IN NONDIABETICS WITH HEPATIC DISEASE

1959

ChlorpropamideChlorpropamidemedicine.medical_specialtybusiness.industryLiver DiseasesGeneral NeuroscienceMEDLINEDiseasemedicine.diseaseGeneral Biochemistry Genetics and Molecular BiologyHistory and Philosophy of ScienceDiabetes mellitusInternal medicineDiabetes MellitusmedicineHypoglycemic Agentsbusinessmedicine.drugAnnals of the New York Academy of Sciences
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Coupling of Cholesterol and Cone-shaped Lipids in Bilayers Augments Membrane Permeabilization by the Cholesterol-specific Toxins Streptolysin O and V…

2001

Abstract Vibrio cholerae cytolysin (VCC) forms oligomeric pores in lipid bilayers containing cholesterol. Membrane permeabilization is inefficient if the sterol is embedded within bilayers prepared from phosphatidylcholine only but is greatly enhanced if the target membrane also contains ceramide. Although the enhancement of VCC action is stereospecific with respect to cholesterol, we show here that no such specificity applies to the two stereocenters in ceramide; all four stereoisomers of ceramide enhanced VCC activity in cholesterol-containing bilayers. A wide variety of ceramide analogs were as effective asd-erythro-ceramide, as was diacylglycerol, suggesting that the effect of ceramide …

Cholera ToxinCeramideCell Membrane PermeabilityLipid BilayersBiologyCeramidesBiochemistrychemistry.chemical_compoundBacterial ProteinsPhosphatidylcholineLipid bilayerNuclear Magnetic Resonance BiomolecularVibrio choleraeMolecular BiologyDiacylglycerol kinaseCytotoxinsCell BiologyLipid MetabolismLipidsSphingolipidSterolCholesterolchemistryBiochemistryStreptolysinslipids (amino acids peptides and proteins)StreptolysinCytolysinJournal of Biological Chemistry
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A novel cholesterol-based detergent

2005

Design, synthesis and characterization of CHAPSTEROL, a novel cholesterol-based detergent developed for functional solubilization of cholesterol-dependent membrane proteins are described. To validate CHAPSTEROL, we employed the oxytocin receptor, a G protein-coupled receptor requiring cholesterol for its high-affinity binding state. Using the photoactivatable cholesterol analogue [3H]6,6-azocholestan-3beta-ol[3alphaH], we demonstrate that solubilization by CHAPSTEROL leads to an enrichment of cholesterol-binding proteins whereas the widely used bile acid derivative CHAPSO leads to a significant depletion of cholesterol-binding proteins. Similar to Triton X-100 and CHAPS, CHAPSTEROL maintain…

CholesterolCell BiologyBiologyBiochemistrychemistry.chemical_compoundMembraneBiochemistryMembrane proteinchemistryChapsCaveolinlipids (amino acids peptides and proteins)SphingomyelinMolecular BiologyLipid raftPolyacrylamide gel electrophoresisFEBS Journal
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Partial vinylphenol reductase purification and characterization from Brettanomyces bruxellensis

2008

International audience; Brettanomyces is the major microbial cause for wine spoilage worldwide and causes significant economic losses. The reasons are the production of ethylphenols that lead to an unpleasant taint described as 'phenolic odour'. Despite its economic importance, Brettanomyces has remained poorly studied at the metabolic level. The origin of the ethylphenol results from the conversion of vinylphenols in ethylphenol by Brettanomyces hydroxycinnamate decarboxylase. However, no information is available on the vinylphenol reductase responsible for the conversion of vinylphenols in ethylphenols. In this study, a vinylphenol reductase was partially purified from Brettanomyces bruxe…

Chromatography GasBrettanomycesMolecular Sequence DataVINYLPHENOL REDUCTASEBrettanomyces bruxellensisWineReductaseMicrobiology[ CHIM ] Chemical SciencesFungal Proteins03 medical and health sciencesHydrolysisOpen Reading FramesPhenolsOxidoreductaseGenetics[CHIM]Chemical SciencesAmino Acid SequenceMolecular Biology030304 developmental biologychemistry.chemical_classificationWineVOLATILE PHENOL0303 health sciencesbiology030306 microbiologyChemistryGuaiacolTemperatureBRETTANOMYCESHydrogen-Ion Concentrationbiology.organism_classificationNADAmino acidMolecular WeightKineticsEnzymeBiochemistryDETERIORATION MICROBIENNESaccharomycetalesBRUTTANOMYCES BRUXELLENSISFood MicrobiologyElectrophoresis Polyacrylamide GelOxidoreductases
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Simultaneous analysis of lysine, Nɛ-carboxymethyllysine and lysinoalanine from proteins

2007

Protein quality was assayed by simultaneous measurement of lysine (Lys), carboxymethyllysine (CML) and lysinoalanine (LAL). GC-FID analysis of N-tert-butyl dimethylsilyl (tBDMSi) derivatives of these amino acids was undertaken. tBDMSi derivates were separated on a CP-SIL 5CB commercially fused silica capillary column (25 m × 0.25 mm i.d., 0.25 μm film thickness) employing a thermal gradient programmed from 200 to 300 °C. The identity of tBDMSi derivatives of Lys, CML and LAL was established by GC–MS while FID detection was employed for quantification. Analytical parameters such as linearity (lysine 350–4200 μM, LAL 3–81 μM, CML 16–172 μM), precision (1–13% variation coefficients), accuracy …

Chromatography GasG proteinEggsFluoroacetatesClinical BiochemistryLysineLysinoalanineBiochemistryAnalytical Chemistrysymbols.namesakeCaseinAcetamidesOrganosilicon CompoundsNɛ-CarboxymethyllysineLysinoalanineSoy proteinchemistry.chemical_classificationGas chromatographyChromatographyChemistryLysineProteinProteinsCell BiologyGeneral MedicineGlutenMaillard ReactionMaillard reactionsymbolsInfant FoodProtein qualityFood Analysis
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