A trypsin enzyme assay was performed by mixing 50 µL of trypsin with 950 µL of substrate in a cuvette with a pathlength of 1.00 cm. The absorption coefficient for the product formed by this reaction at 480 nm is 4130 M-'cm'. The rate of change in absorbance at 480 nm was 0.129 abs/min. What is the rate of this reaction in units of µmol/min?

A trypsin enzyme assay was performed by mixing 50 µL of trypsin with 950 µL of substrate in a cuvette with a pathlength of 1.00 cm. The absorption coefficient for the product formed by this reaction at 480 nm is 4130 M-'cm'. The rate of change in absorbance at 480 nm was 0.129 abs/min. What is the rate of this reaction in units of µmol/min?

Principles of Instrumental Analysis

7th Edition

ISBN:9781305577213

Author:Douglas A. Skoog, F. James Holler, Stanley R. Crouch

Publisher:Douglas A. Skoog, F. James Holler, Stanley R. Crouch

Chapter32: Radiochemical Methods

Section: Chapter Questions

Problem 32.18QAP: The streptomycin in 500 g of a broth was determined by addition of 1.25 mg of the pure antibiotic...

See similar textbooks

Similar questions

A solution of Tryptophan has an absorbance at 280 nm of 0.54 in a 0.5 cm length cuvette. Given the absorbance coefficient of trp is 6.4 x 103 Lmol-1cm-1. What is the concentration of solution?
A 20 ppm solution of a DNA molecule (unknown molecular weight) isolated from Escherichia coli was found to an absorbance of 0.80 in a 2-cm cell. Calculate the absorptivity of the molecule.
The kinetics of hydrolysis of acetylsalicylic acid (aspirin) under certain conditions of temperature, pH, type of buffer and strength ionic, can be followed by multicomponent spectrophotometry. When performing a calculation of optical constants, the following data were obtained: Solution C. mg/100 mL A in λ (276nm) A in λ (290nm) Ac. acetylsalicylic ( AAS) 0.202 0.102 0.031 Ac. salicylic (AS) 0.198 0.158 0.101 Reaction: AAS + H2O → AS + CH3COOH In a kinetic study, after a certain time, 1 mL of the solution was taken from the reactor and diluted to 10 mL with water. distilled. Then when proceeding to the spectrophotometric measurement, the last solution presented the absorbances of 0.244 and 0.102 for the lengths of 276 and 290 nm respectively. What are the concentrations of ASA and AS in mg/L, at that instant in the reactor? Note: Acetic acid does not absorb at either wavelength.
At 21 °C, a solution of 12 mL each of 0.00200 M Fe3+ and 0.001000 M SCN- was mixed and brought to 25.0 mL with 0.1 M HNO3. The absorbance at 450 nm was measured to be 0.350 (A450 = 0.350). This solution was then heated to 45 °C and the absorbance at 450 nm was measured to be 0.142 (A450= 0.142). Is the reaction: Fe3+(aq) + SCN -(aq) → FeSCN2+(aq) exothermic or endothermic? Explain.
You have measured the blank for a determination of arsenic in food samples by hydride-generation atomic fluorescence spectrometry. The blank values are: 0.23 ppb, 0.14 ppb, 0.16 ppb, 0.28 ppb, 0.18 ppb, 0.09 ppb, 0.10 ppb, 0.20 ppb, 0.15 ppb, 0.21 ppb As. What is the LOD?
The biuret reaction is a general method for the determination of proteins or peptides. This method is based on the reaction of the Cu2+ with four NH groups of the peptide bonds, forming a violet complex with an absorption maximum at 540 nm. The intensity of the color is proportional to the number of peptide bonds present, and therefore to the amount of protein. This reaction is specific, the dipeptides and amino acids give a negative reaction, and few substances interfere. A quantity of 19.89 g of fish meat is extracted with 100 mL of glacial acetic acid. Subsequently, 3 mL of the previous solution with 3 mL of the biuret reagent to generate the reaction, after 30 minutes. To reduce errors due to other interfering substances and residual turbidity, the corrected absorbance method Ac is applied to 500 nm and 570 nm. In a study, a standard sample analyzed by the Kjeldahl method (total Nitrogen analysis) is obtained, resulting in 0.43% N (w / v), (Protein content [%] =% N x 6.38). 3 mL of…
Calculate the (a) Linearity constant (r), (b) y-intercept, (c) Slope, and (d) Protein content of an unknown sample having an absorbance of 0.325.
A student conducted an experiment to determine the concentration of benzene in an ethanol solution. Use the UV spectrum of the solution in a 2.0 cm cell. Within the spectrum, there was a peak attributed to benzene at 260 nm, with an absorption of 0.69. In a reference source, the student found that the adsorption of the benzene strip with ethanol was 2.95 x 10-3 ppm cm-. What is the molar concentration of benzene in the sample (mm of benzene = 78.11 g/mol)
. A student collects the following data for the absorbance of a complex measured in 1.00 cmspectrophotometric cells. The molar absorptivity (ε) of the complex under investigation is 2.25×103L/mol·cm. Calculate the concentration of the complex in solution at each time of the reaction.Time (min)MeasuredAbsorbanceComplex Concentration(M)0.000 1.50010.000 1.31320.000 1.12530.000 0.93840.000 0.750
what is the concentration of the unknown sample using serial diluitions: 0.05M 1.7472nm, 0.025M 0.8569nm, 0.0125M 0.4167nm, 0.00625M 0.1958nm the epsilon value is 0.0101 and l is 1 cm
The absorption coefficient of rhodopsin at 496 nm is 40,000 M-1cm-1. If you have a 1M solution of rhodopsin, how many times will you dilute the solution so that the diluted solution will give you an absorption reading at 496 nm that is in the range of 0.1-1.0. And what will be the absorption by the diluted solution?
Calculate the absorbance at 280 nm that is expected for a 17 microM solution of peptide GRAYISH, if a 10-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.