Search results for "molecular mass"

showing 10 items of 155 documents

Onco-fetal/laminin-binding collagen from colon carcinoma: detection of new sequences.

1995

We have recently identified an oncofetal-laminin binding collagen (OF/LB) composed of three alpha chains, with the apparent molecular mass of about 100 kDa each, but bearing different pI. One of the chains appears markedly acidic in a bidimensional electrophoretic system, where the NEPHGE is used as first dimension separating gel, while the two more basic chains have similar migration as alpha 1(III) and alpha 1(I) collagen chains, respectively. Sequence analyses have been performed on CNBr-peptides, derived from pepsinized triple helical molecules and on tryptic fragments obtained after in gel digestion of the acidic band. The research of sequence homology with computerized databases indic…

Macromolecular SubstancesBiopsyMolecular Sequence DataBiophysicsSequence (biology)In-gel digestionBiochemistryMoleculeHumansElectrophoresis Gel Two-DimensionalTrypsinAmino Acid SequenceCyanogen BromideLaminin bindingMolecular BiologyGeneChromatography High Pressure LiquidFetusMolecular massSequence Homology Amino AcidChemistryCell BiologyMolecular biologyPeptide FragmentsElectrophoresisBiochemistryColonic NeoplasmsCollagenBiochemical and biophysical research communications
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Purification, subunit structure, and kinetics of the chloroform-released F1ATPase complex from Rhodospirillum rubrum and its comparison with F1ATPase…

1979

Abstract A stable and homogeneous adenosine-5ʹ-triphosphatase (ATPase, EC 3.6.1.3) has been solubilized from Rhodospirillum rubrum (R . rubrum) chromatophores by chloroform extraction. Purification of the Ca2+-dependent ATPase activity was 200-fold. Ca2+ can be replaced by Mg2+, Cd2+, and Mn2+ .The Km for Ca-ATP (0.17 mᴍ) is increased about 5-fold during solubilization of the enzyme, whereas the Km values for Mg-ATP (0.029 mᴍ) and Cd-ATP (0.014 mᴍ) are not affected. The chloroform-released ATPase has a molecular weight of 400,000 ± 30,000 and consists of the following subunits (molecular weights in parenthesis): α (58,000), β (53,500), γ (39,000), δ (18,500), and ε (14,000). The amino acid …

Macromolecular SubstancesProtein subunitATPaseRhodospirillum rubrumGeneral Biochemistry Genetics and Molecular Biologychemistry.chemical_compoundAffinity chromatographyAmino AcidsAdenosine TriphosphatasesChloroformChromatographyMolecular massbiologyRhodospirillum rubrumATPase complexBacterial Chromatophoresbiology.organism_classificationMolecular WeightKineticsSpectrometry FluorescencechemistryOxidative Phosphorylation Coupling Factorsbiology.proteinSolventsTriphosphataseChloroformZeitschrift fur Naturforschung. Section C, Biosciences
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Tyrosinases from crustaceans form hexamers

2002

Tyrosinases, which are widely distributed among animals, plants and fungi, are involved in many biologically essential functions, including pigmentation, sclerotization, primary immune response and host defence. In the present study, we present a structural and physicochemical characterization of two new tyrosinases from the crustaceans Palinurus elephas (European spiny lobster) and Astacus leptodactylus (freshwater crayfish). In vivo, the purified crustacean tyrosinases occur as hexamers composed of one subunit type with a molecular mass of approx. 71kDa. The tyrosinase hexamers appear to be similar to the haemocyanins, based on electron microscopy. Thus a careful purification protocol was…

Macromolecular SubstancesProtein subunitTyrosinasePalinurus elephasAstacoideaBiologyAstacus leptodactylusBiochemistryEvolution MolecularSpecies SpecificityCrustaceaHemolymphAnimalsMolecular BiologyMolecular massMonophenol MonooxygenaseEcologyCell BiologyChromatography Ion Exchangebiology.organism_classificationCrayfishKineticsMicroscopy ElectronBiochemistryArthropodSpiny lobsterResearch ArticleBiochemical Journal
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Properties of the F0F1 ATPase Complex from Rhodospirillum rubrum Chromatophores, Solubilized by Triton X-100

1979

1. A cold-stable oligomycin-sensitive F0F1 ATPase complex from chromatophores of Rhodospirillum rubrum FR 1 was solubilized by Triton X-100 and purified by gel filtration. 2. The F0F1 complex is resolved by sodium dodecyl sulfate electrophoresis into 14 polypeptides with approximate molecular weights in the range of 58000--6800; five of these polypeptides are derived from the F1 moiety of the complex which carries the catalytic centers of the enzyme. 3. The purified F0F1 complex is homogeneous according to analytical ultracentrifugation and isoelectric focusing. 4. The molecular weight as determined by gel filtration is about 480 000 +/- 30 000. S020,w is 1.45 +/- 0.1 S and the pI is 5.4. 5…

Macromolecular SubstancesSize-exclusion chromatographyRhodospirillum rubrumBiochemistryPolyethylene GlycolsSubstrate SpecificityDivalentchemistry.chemical_compoundMoietyAmino AcidsSodium dodecyl sulfateAdenosine Triphosphataseschemistry.chemical_classificationChromatographyMolecular massbiologyChemistryIsoelectric focusingRhodospirillum rubrumBacterial Chromatophoresbiology.organism_classificationMolecular WeightKineticsOxidative Phosphorylation Coupling FactorsTriton X-100OligomycinsEuropean Journal of Biochemistry
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Isolation and characterization of maerophage-derived C1q and its similarities to serum C1q

1986

Recently, we have shown that the collagen-like, Fc-recognizing subcomponent C1q of the first complement component is synthesized by human, guinea pig and mouse peritoneal macrophages. To test whether macrophages may contribute to the serum pool of C1q, C1q was purified from guinea pig serum and from guinea pig peritoneal macrophage supernatants and compared for similarities. Both molecules had a similar sedimentation rate (macrophage C1q: 11.3 S, serum C1q: 11.2 S) and showed on sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing conditions three identical bands with molecular weights of Mr, 29 000, Mr, 27 000 and Mr 23 000 for the A, B and C chains, respectively. Both …

MaleComplement Activating EnzymesGuinea PigsImmunologychemical and pharmacologic phenomenaImmunoelectrophoresisBiologyurologic and male genital diseasesChromatography AffinityGuinea pigfluids and secretionsAntigenimmune system diseasesmedicineAnimalsImmunology and AllergyMacrophageskin and connective tissue diseasesComplement C1qGel electrophoresisMolecular massmedicine.diagnostic_testComplement C1qMacrophagesOuchterlony double immunodiffusionBiochemistryFemaleEuropean Journal of Immunology
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A discoidal lipoprotein from the coelomic fluid of the polychaete Nereis virens.

2005

A discoidal lipoprotein was isolated from the coelomic fluid of the polychaete, Nereis virens, by density gradient centrifugation. The lipoprotein was present in both sexes and moved as a uniform band in an agarose gel. The average diameter of the lipoprotein particles determined by electron microscopy was 42 nm with a thickness of 10 nm. SDS electrophoresis showed two apoprotein subunits with molecular masses of 247 and 85 kDa, respectively. In lectin blots, both apoproteins were reactive with Concanavalin A indicating the presence of N-glycans. The small subunit was also reactive with peanut lectin, indicating additional O-glycosylation. The total lipid content was 48% and consisted mainl…

MaleEmbryo NonmammalianGlycosylationPhysiologyLipoproteinsBiologyIn Vitro TechniquesBiochemistrychemistry.chemical_compoundPolysaccharidesAnimalsParticle SizeMolecular BiologyDifferential centrifugationMolecular massLectinPolychaetaLipidsThin-layer chromatographyBody FluidsMolecular WeightElectrophoresisProtein SubunitschemistryBiochemistryConcanavalin Abiology.proteinAgaroselipids (amino acids peptides and proteins)FemaleLipoproteinComparative biochemistry and physiology. Part B, Biochemistrymolecular biology
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A novel pyruvate kinase (PK-S) from boar spermatozoa is localized at the fibrous sheath and the acrosome

2007

Boar spermatozoa contain a novel pyruvate kinase (PK-S) that is tightly bound at the acrosome of the sperm head and at the fibrous sheath in the principal piece of the flagellum, while the midpiece contains a soluble pyruvate kinase (PK). PK-S could not be solubilized by detergents, but by trypsin with no loss of activity. Purified PK-S as well as PK-S still bound to cell structures and soluble sperm PK have all kinetics similar to those of rabbit muscle PK-M1. The PK-S subunit had a relative molecular mass of 64 ± 1 × 103(n= 3), i.e. slightly higher than that of PK-M1, and carried an N-terminal extension (NH2-TSEAM-COOH) that is lacking in native PK-M1. Evidence is provided that PK-S is en…

MaleEmbryologyErythrocytesSwineProtein subunitBlotting WesternMolecular Sequence DataPyruvate KinaseBiologyEndocrinologySpecies SpecificitymedicineAnimalsAmino Acid SequenceAcrosomeSequence Homology Amino AcidMolecular massAntibodies MonoclonalObstetrics and GynecologyCell BiologyImmunogold labellingTrypsinSpermatozoaSpermReproductive MedicineBiochemistryPolyclonal antibodiesSperm Tailbiology.proteinElectrophoresis Polyacrylamide GelRabbitsSperm MidpieceAcrosomePyruvate kinasemedicine.drugReproduction
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Purification and characterization of rat-liver cytosolic epoxide hydrolase.

1988

Rat liver cytosolic epoxide hydrolase has been purified and characterized. The enzyme was purified from tiadenol-induced rat liver 540-fold with respect to trans-stilbene oxide as a substrate. Similar purification was obtained with the substrates trans-beta-ethyl styrene oxide and styrene 7,8-oxide, the specific activities decreasing in the order trans-beta-ethyl styrene oxide greater than styrene 7,8-oxide greater than trans-stilbene oxide. The enzyme exerts highest activity at pH 7.4 Km and Vmax of the pure enzyme for trans-stilbene oxide were 1.7 microM and 205 nmol x min-1 x mg protein-1 respectively. With trans-stilbene oxide as a substrate, the inhibition by organic solvents (2.5% by …

MaleGuinea PigsBiologyBiochemistryPeptide MappingStyreneSubstrate Specificitychemistry.chemical_compoundMiceCytosolStyrene oxideAnimalsIsoelectric PointEpoxide hydrolasechemistry.chemical_classificationEpoxide HydrolasesMolecular massHydrolysisImmunochemistrySubstrate (chemistry)Rats Inbred StrainsHydrogen-Ion ConcentrationRats Inbred F344RatsMice Inbred C57BLMolecular WeightEnzymechemistryBiochemistryLiverMicrosomal epoxide hydrolaseMicrosomeMicrosomes LiverSolventsPeptide HydrolasesEuropean journal of biochemistry
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The major isozyme of rat cardiac glutathione transferases. Its correspondence to hepatic transferase X.

1986

1. A major isozyme of rat heart glutathione transferase was purified to homogeneity by Sephadex G-200 gel filtration, ammonium sulfate precipitation, CM-cellulose chromatography and affinity chromatography on S-hexylglutathione-linked Sepharose 6B. 2. The purified isozyme was a dimer with an apparent relative molecular mass of 50000 composed of two Yb-size subunits (Mr= 26 500). The isozyme is immunologically related to rat liver glutathione transferase X and 3–3, especially closely to transferase X, and no immunological cross-reactivity with subunits 1 and 2 of hepatic glutathione transferases was observed. The isoelectric point (pI = 6.9) of the isozyme was identical with and the substrat…

MalePyruvate dehydrogenase lipoamide kinase isozyme 1ImmunodiffusionBiologyBiochemistryIsozymeChromatography AffinitySubstrate SpecificitySepharosechemistry.chemical_compoundAffinity chromatographyTransferaseAnimalsIsoelectric PointGlutathione TransferaseMolecular massMyocardiumRats Inbred StrainsGlutathioneHydrogen-Ion ConcentrationMolecular biologyRatsIsoenzymesMolecular WeightIsoelectric pointchemistryBiochemistryLiverChromatography GelElectrophoresis Polyacrylamide GelEuropean journal of biochemistry
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Glutathionyl-biliverdin IXα, a new heme catabolite in a marine annelid: Sex and cell specific accumulation.

2011

Abstract We have isolated and characterized the green pigment accumulating in coelomic cells (eleocytes) of the common clam worm Nereis virens by means of RP-HPLC and ESI-tandem mass spectrometry. This pigment is a novel biliverdin-glutathione conjugate in which the glutathione is linked to the biliverdin-backbone via a thioether bond. The yolk precursor vitellogenin, a female-specific high-density lipoprotein ( ρ  = 1179 kg/m 3 ) with a native molecular mass of ∼500 kDa and a subunit mass of ∼150 kDa, is capable of transporting this pigment as well as heme. The sex-independent large discoidal lipoprotein present in the coelomic fluid, which is sequestered by the eleocytes, could also be sh…

Malefood.ingredientProtein subunitHemeBiochemistrychemistry.chemical_compoundVitellogeninfoodYolkAnimalsHemeSex CharacteristicsBiliverdinMolecular massbiologyBiliverdinePolychaetaGeneral MedicineGlutathioneGlutathionechemistryBiochemistrybiology.proteinlipids (amino acids peptides and proteins)FemaleHemoglobinBiochimie
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