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What is the assay method of telmisartan , with illustration?
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- Search the standard of Bendroflumethiazide and its tablets USP. •What kind of method applied in the assay of Bendroflumethiazide and its tablets respectively? •Why use different method for API and preparation? •Find some other method for the quantification of Bendroflumethiazide.My Professors asked me to make a standard curve for Gallic acid and she asked me to follow the triplicate basis and make the curve straight line. After i done my analysis i Found these values( absorbance)which i attached below. Can you please make a standard curve from these values? If my values are inaccurate to form a standard curve straight line, please also provide the desired data Which will form a straight line. Please help me ,it will be kind. I will rate you positive if you do so. Please please. ...Calculate the concentration of a solution of peptide AWSME, in mM if the absorbance at 280 nm for the solution is 0.6 absorbance units, and a 0.2-cm cuvette is used. For the extinction coefficient, take into account that e280(Trp) = 5690 M-1 cm-1 and e280(Tyr) = 1280 M-1 cm-1. Round your answer to two decimals.
- I need some help assessing the spectra of maleic anhydride how do I determine the integration, multiplicity, chemical shift for each structure/ fragment part of the maleic anhydrideApplying the best-fit method you produce the following plot. Please select the correct statement. Group of answer choices: 1. The Bradford assay gives a hyperbolic plot for absorbance versus protein concentration. 2. The Bradford assay is measured at at absorbance of 600 nm 3. Within a range of relatively low protein concentrations, the hyperbolic curve can be approximated reasonably well by a straight line.Thiamine is assayed by? I. Spectrophotometry II. Fluorometry III. Turbidimetry A. I, II and III B. I and II only C. II only D. I only
- What is the difference between molecular ion peak and base peak.help pleaseI did not understand soultion for the question.. The relationship between Affinity and Association & Dissociation Constant. Four proteins (A-D) all bind the same ligand (X), with different affinities. For protein A & B we know that they have a binding site for X with a Kd (dissociation constant) of 10⁻⁵and 10⁻⁸ M, respectively. For protein C and D we know that they have a binding site for ligand X with a Ka (association constant) of 10³and 10⁵M, respectively. Which protein has the highest affinity for ligand ? Explain your reasoning. How do you make them all in same constant so that values can be compared and the one with highest Ka or lowest Kd (Highest affinity in both cases) can be ruled out.
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