Search results for "Isosbestic point"

showing 3 items of 3 documents

Interpretation and Chemometric Evaluation of the Bilirubin Interference in the Kinetic Spectrophotometry Determination of Creatinine in Serum by Use …

1992

Abstract SUMMARY In an alkaline picrate medium we demonstrated the occurrence of isosbestic points over the range 520–550 nm, the position depending on the bilirubin content and less on the albumin content. Bilirubin does not markedly modify the ratt constant of the reaction between creatinine and picrate, however, it does modify the intercept of the Ln ΔA vs t, plots. The absolute value of Ln ΔA varies with the concentration, though not with time, which indicates that bilirubin acts by consuming part of the initially present creatinine irrespective of its owr concentration at the wavelengths typically used in the creatinine determination. The Ln ΔA values at the isosbestic points coincide …

Isosbestic pointCreatininemedicine.diagnostic_testBilirubinPicrateBiochemistry (medical)Clinical BiochemistryAnalytical chemistryAlbuminKinetic energyBiochemistryAnalytical Chemistrychemistry.chemical_compoundchemistrySpectrophotometryElectrochemistrymedicineAbstract SummarySpectroscopyAnalytical Letters
researchProduct

The Determination of the Reaction Rate for the First Step in a Consecutive Reaction A → B → C by Absorbance Measurements Using the Wavelength of the …

1977

Kinetic experiments are often followed by spectroscopic measurements in the visible or near ultraviolet region. The advantage is not only that the results can be recorded continuously, which makes very fast reactions accessible, but also that very low concentrations of substrates can be used. This means that only very small amounts are required and, more important perhaps, that reagents can be used in excess. Thus pseudomonomolecular conditions and first-order kinetics often can be achieved easily.

Isosbestic pointReaction rateAbsorbanceWavelengthChemistryReagentKineticsAnalytical chemistryNear ultravioletKinetic energyInstrumentationSpectroscopyApplied Spectroscopy
researchProduct

On the molecular structure of human neuroserpin polymers

2012

The polymerization of serpins is at the root of a large class of diseases; the molecular structure of serpin polymers has been recently debated. In this work, we study the polymerization kinetics of human neuroserpin by Fourier Transform Infra Red spectroscopy and by time-lapse Size Exclusion Chromatography. First, we show that two distinct neuroserpin polymers, formed at 45 and 85°C, display the same isosbestic points in the Amide I' band, and therefore share common secondary structure features. We also find a concentration independent polymerization rate at 45°C suggesting that the polymerization rate-limiting step is the formation of an activated monomeric species. The polymer structures…

Models MolecularSize-exclusion chromatographySerpinBiochemistryProtein Structure Secondaryserpinopathieprotein aggregationchemistry.chemical_compoundStructural BiologyNeuroserpinCatalytic DomainSpectroscopy Fourier Transform InfraredPolymer chemistryHumansMolecular BiologyProtein secondary structureSerpinschemistry.chemical_classificationIsosbestic pointChemistryNeuropeptidesserpinPolymerSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)KineticsCrystallographyMonomerprotein aggregation; serpins; serpinopathies; serpin polymerization; FTIRPolymerizationFTIRChromatography GelProtein Multimerizationserpin polymerization
researchProduct