1. An obstruction in blood flow to the kidneys would result in
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A. |
increased erythropoiesis. |
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B. |
reduced release of renin from the juxtaglomerular cells |
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|
C. |
pernicious anemia. |
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D. |
increased glucose clearance |
2. Why do you need parietal cells in your stomach to produce red blood cells?
A.The stomach is needed for nutrition, and you need amino acids and iron to make red blood cells.
B.Iron (Fe2+) is absorbed in the stomach by parietal cells
C.Parietal cells secrete intrinsic factor, which is necessary to absorb vitamin B12 in the small intestine.
D.Parietal cells secrete intrinsic factor that binds Fe2+, allowing it to be absorbed in the small intestine.
3. What is true about a person with a Rh- blood type?
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A. |
She is a universal acceptor. |
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|
B. |
If she has an Rh-negative baby that baby might have hemolytic disease of the newborn. |
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C. |
She has anti-Rh antibodies in her plasma. |
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D. |
She has Rh antigens on her red blood cells. |
In: Anatomy and Physiology
In: Anatomy and Physiology
Download the Perl code of "Example 1: Conceptual Translation" from "Resources for Undergraduate Bioinformatics Instruction" at Wright State University http://birg.cs.wright.edu/resources/index.shtml. The program performs the conceptual translation on three forward reading frames from mRNA nucleotides to amino acids. The mRNA sequence is provided as the command line argument. Modify it to add the following features:
a. (5pts) If no argument is provided in the command line, prompt
the user to input a nucleotide sequence. Note that the modified
code should still take the command line argument if present.
done
b. (5pts) Accept lower case letters. done
c. (5pts) Accept a DNA sequence as the input. That is, thymine
(T or t), should also be valid in the input.
d. (10pts) Perform the conceptual translation on the three backward
reading frames in addition to on the forward reading frames.
Note that:
You are not allowed to modify the hash table provided in the code of Example 1.
The code is required to utilize the binding operator =~ whenever possible
instead of loops.
In: Computer Science
The absorbance of a 1 mg/ml sample of lysozyme was measured in a cuvette of thickness 1.00 cm and was found to be 3.19 at 240 nm and 2.58 at 280 nm. The molar absorption coefficients of tryptophan and tyrosine at 240 nm are 2.00 x 103 dm3 mol-1 cm-1 and 1.12 x 104 dm3 mol-1 cm-1, respectively, and at 280 nm they are 5.40 x 103 dm3 mol-1 cm-1 and 1.50 x 103 dm3 mol-1 cm-1, respectively. What are the molar concentrations of the two amino acids in the 1 mg/ml protein sample? If the molar mass of the protein is 14,400 g/mol, how many tryptophans and tyrosines are present in the sequence of this protein? (looking for the molar ratio, moles aa/mol protein) What is the molar absorption coefficient of the lysozyme protein at 280 nm? What would be the % Transmittance of the same protein sample if measurements were made in a 0.1 cm cuvette at 280 nm?
In: Chemistry
Regulation of gene expression occurs primarily at the level of transcription. What would be different if cells controlled gene expression primarily at the level of translation?
| a. |
The ability to rapidly respond to environmental change would be reduced. |
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| b. |
Genes would no longer be transcribed efficiently. |
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| c. |
Cells would expend significantly more energy. |
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| d. |
Many different protein isoforms would be produced. |
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| e. |
Translation of mRNA would not occur. |
If an enhancer associated with a gene was deleted or mutated, what would be the effect on levels of gene expression?
| a. |
Gene expression would be reduced or not occur at the appropriate time. |
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| b. |
The gene would not be recognized by RNA polymerase. |
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| c. |
Gene expression would not occur at all. |
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| d. |
Gene expression would increase or occur at the inappropriate time. |
Cells regulate gene expression at the level of translation by:
| a. |
controlling ribosome binding at the 5' end of mRNA. |
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| b. |
controlling the length of the polyA tail. |
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| c. |
controlling the amount of amino acids used. |
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| d. |
a and b |
|
| e. |
a, b and c |
|
| f. |
a and c |
In: Biology
In: Biology
Using 1.0 nM enzyme X for the enzyme kinetics experiments, you obtained the reaction rates at different concentrations of substrate (shown in the following table). Assume that the enzyme X follows a typical Michaelis-Menten kinetics.
[substrate] (μM) Reaction rate (μmol/min)
2 7
5 17
10 29
20 44
50 67
100 80
200 89
500 95
1000 98
a) Estimate the Vmax and Km values of the enzyme in this reaction using double reciprocal plot.
b) If 5.0 nM of the enzyme X is used in the experiment, what will be the Vmax and Km of the enzyme X?.
In: Chemistry
Using 1.0 nM enzyme X for the enzyme kinetics experiments, you obtained the reaction rates at different concentrations of substrate (shown in the following table). Assume that the enzyme X follows a typical Michaelis-Menten kinetics.
[substrate] (μM) Reaction rate (μmol/s)
2 7
5 17
10 29
20 44
50 67
100 80
200 89
500 95
1000 98
a) Estimate the Vmax and Km values of the enzyme X in this reaction using the double reciprocal plot.
b) If 5.0 nM of the enzyme X is used in the experiment, what will be the Vmax and Km values of the enzyme X?
In: Chemistry
Which of the following would be expected to lower the Tm for a phospholipid bilayer?
replacing a lipid containing unsaturated fatty acids with one containing saturated fatty acids.
replacing a lipid containing 18-C fatty acids with one containing 16-C fatty acids.
adding ions to bind to charged groups in the polar head groups.
decreasing the concentration of phospholipids.
In: Chemistry
elemental analysis of an unknown compound was found to give the following data 70.4% carbon, 8.08% hydrogen and 10.12 % of nitrogen. it was found to have a molecular weight of 137.18 Da. determine the empirical formula, molecular formula, and the degree of unsaturation for this compound
In: Chemistry