Mammalian cells growing in culture were labeled with [3H]-thymidineto estimate the rate of DNA synthesis. The thymidine administered had aspecific activity of 3000 cpm/pmol. At intervals, samples of culture weretaken and acidified to precipitate nucleic acids. The rate of incorporation ofisotope into DNA was 1500 cpm/106 cells /min. A portion of culture wastaken to determine the specific activity of the intracellular dTTP pool, whichwas found to be 600 cpm/pmol.(a) What fraction of the intracellular dTTP is synthesized from the exogenous precursor?(b) What is the rate of DNA synthesis, in molecules per minute per cell ofthymine nucleotides incorporated into DNA?(c) How could you determine the specific activity of the dTTP pool?

Mammalian cells growing in culture were labeled with [3H]-thymidineto estimate the rate of DNA synthesis. The thymidine administered had aspecific activity of 3000 cpm/pmol. At intervals, samples of culture weretaken and acidified to precipitate nucleic acids. The rate of incorporation ofisotope into DNA was 1500 cpm/106 cells /min. A portion of culture wastaken to determine the specific activity of the intracellular dTTP pool, whichwas found to be 600 cpm/pmol.(a) What fraction of the intracellular dTTP is synthesized from the exogenous precursor?(b) What is the rate of DNA synthesis, in molecules per minute per cell ofthymine nucleotides incorporated into DNA?(c) How could you determine the specific activity of the dTTP pool?

Curren'S Math For Meds: Dosages & Sol

11th Edition

ISBN:9781305143531

Author:CURREN

Publisher:CURREN

Chapter10: Reconstitution Of Powdered Drugs

Section: Chapter Questions

Problem 8.1P

See similar textbooks

Similar questions

A vial of Doxorubicin reads 0•5g per vial. Instructions say to reconstitute each 12mg with 2•5ml of NS. How many ml of NS will be needed to reconstitute the vial of the recommended concentration? please show working
In a nutrient medium that lacks histidine, a thin layer of agar containing ~109 Salmonella typhimurium histidine auxotrophs (mutant cells that require histidine to survive) produces ~13 colonies over a two-day incubation period at 37 °C. How do these colonies arise in the absence of histidine? The experiment is repeated in the presence of 0.4 μg of 2-aminoanthracene. The number of colonies produced over two days exceeds 10,000.What does this indicate about 2-aminoanthracene? What can you surmise about its carcinogenicity?
Given this, if you used 6g of vitamin Z powder to make 20 ml of solution, what is the % concentration of this solution? (I gave the image since I don't know if that info is needed to solve this question.)It also gives a follow-up, if you can help here too: You work in a lab as a summer student. One of your tasks is to make sure that there is enough cell culture medium containing antibiotics to grow bacteria. One day you realize that there is only 5 ml of 10% Antibiotic stock solution in the freezer. You decide to use it all to prepare the working culture medium with 0.01% antibiotic. In the lab there is plenty of growth medium without antibiotics. (Note: dilution in medium is like dilution in water). You remember the equation to make dilutions of stock solutions. You usually use this formula to calculate the required volume of a stock solution, but you realize it can apply here as well, even though the unknown is the final volume. So, you make that dilution. Given that each bacterial…
Rabbits were in injected with [32 P] photsphate intraperitoneally ans asacrificed after 2, 5, 8, 12, 18, 24, 48, or 168 hours of radioisotope administration. DNA, nuclear RNA (nRNA), and cytoplasmic RNA (cRNA) were prepared from the kidneys and their specific activities (radioactivity/ mg of nucleic acid) were determined 1. what process was studied in this expereiement 2. What is concluded about the division of kideny cells during the time of labeling and why.
In the Lysozyme purification, if the specific activity in the elate was 108 units/mg and the specific activity in the starting material (egg white) was 8 units/mg, what is the purification factor? (To 2 decimal places).
A decapeptide which could resist burns was isolated from an endemic plant from Mt. Mayon. Deduce the amino acid sequence of the decapeptide given the following informations. Mercaptoethanol gave two pentapeptides F1 and F2. Chymotrypsin treatment of F1 releases S and a tetrapeptide (C,K,F,M) while F2 gave a dipeptide (M,S) and a tripeptide (C,F,K) F1 when treated with CNBr released a free homoserine lactone and a tetrapeptide. Trypsin treatment of F1 gave a tripeptide and a dipeptide. F2 treated with carboxypeptidase released free M while with trypsin gave free K and a tetrapeptide.
For the study of alanine production by a recombinant strain of E. coli, cultivation was carried out in a benchtop bioreactor with 4.5 L of culture medium, using glucose as a limiting substrate. During the cultivation, there was no lag phase and the cells showed exponential growth for 5 hours. The following table presents the results of the analysis of ammonia and glucose consumption, and alanine accumulation throughout the cultivation. Knowing that 500 mL of a cell suspension at a concentration of 5.0 g/L (inoculum) was added to the 4.5 L of medium in the reactor and that the YX/NH3 previously determined was 7.5, calculate:a) the maximum specific growth rateb) YX/S and YP/S yield factorsc) How long would it take to reach Cx = 30 g/L if the cells continued with the exponential growth profile until the end of the culture (without nutrient deprivation or any type of inhibition)?d) Describe how the mathematical treatment of the data should be done to determine the type of product formation…
Radioactive uracil can be used to label all the pyrimidine residues in DNA. Explain how this occurs, thinking about pyrimidine synthetic pathways.
You perform a Bradford assay to determine the concentration of isolated α-lactalbumin. You use 50 μL of a two-fold diluted solution of α-lactalbumin in the assay. You generate a standard curve with the following equation for the line: y = 0.163x + 0.082. The absorbance of your sample was 0.674 AU. What is the concentration of α-lactalbumin, in mg/mL, in your sample? Give your answer to three significant figures.
A student performed an invertase activity assay on samples from a purification. All reactions occurred in a reaction volume of 100 µL and lasted 3.1 minutes. For each reaction, 5.00 µL enzyme was mixed with 50.0 mM sucrose in 10.0 mM acetate pH 4.8. Then 400 µL of DNS was added, the samples were heated to 90 °C for 5 minutes, and 500 µL of 50.0 mM acetate pH 4.8 was added before loading a 96 well plate in triplicate. Samples were measured at 540 nm using a path length of 0.680 cm. The fraction with the highest activity had A540 of 0.904. The standard of 14.00 mM hydrolyzed sucrose had A540 of 1.047 (the concentration given is of the 100 µL sample). The no-enzyme control had A540 of 0.174. Calculate the activity of the fraction (in nmol min-1).
protein is purified and at a concentration of 600 μg in 1.75 ml of buffer. You do an assay with your purified protein, and the assay requires 25 μg of biochemisfunase. What volume of the purified biochemisfunase would yield 25 μg? Show your calculation.
A conjugate was incubated with a mixture of lysosomal enzymes and no drug release was observed in these conditions. The same conjugate was tested for antitumor activity in vivo and an anticancer effect was observed. Taking into account the information provided above, hypothesize a possible mechanism of action for this conjugate.