
Concept explainers
To review:
The effects of rigorous exercise on muscle glycogen, blood glucose, and carbohydrate utilization in the given two trials.
Given:
A group of seven trained cyclists was included in two cycling trials. On day 1, the athletes were given flavored water (a placebo) at 20 minutes interval throughout the trial. On day 2, the athletes were administered with glucose, again at every 20 minutes interval throughout the trial. The levels of the muscle glycogen and the time taken by muscles to get tired were recorded and are shown in the Table 1.
Table 1: Time taken by the muscles to get tired in response to different drinks.
Types of drinks ingested by athletes | Levels of muscle glycogen at the starting (0 hours) | Levels of muscle glycogen after 2 hours of cycling | Levels of muscle glycogen after 3 hours of cycling | Levels of muscle glycogen after 4 hours of cycling | Time taken by muscles to get fatigued (hours) |
Flavored water) Place bo | 163 ± 13 | 60 ± 9 | 37 ± 5 | No data | 3.02 ± 0.19 |
Glucose Solution | 173 ± 11 | 71 ± 11 | 44 ± 12 | 39 ± 8 0 | 4.02 ± 0.33 |
P = 0.27 | P = 0.22 | P = 0.30 | P = 0.01 |
Introduction:
Glucose is the source of adenosine triphosphate (ATP) that provides energy by hydrolyzing its phosphate bonds. The glucose is used as a

Explanation of Solution
The probability value (P-value) indicates whether a given data claimed by the experimenter could be accepted or rejected. The data claimed by an experimenter is also known as a null hypothesis. When the P-value is found less than 0.05, the null hypothesis gets rejected. Whereas, if the P-value is found greater than 0.05, the null hypothesis gets accepted.
The given data indicates that glucose level falls after rigorous cycling, but if the glucose is supplied externally, glucose levels were maintained for some time, thereby providing energy. The level of glycogen in muscles remains constant since no breakdown of glycogen is required in case of external administration of glucose. The internal carbohydrates are utilized less frequently because of the presence of externally ingested glucose.
Thus, the P-value greater than 0.05 signifies that the external administration of glucose increase the glucose level in the blood and maintains the muscles’ glycogen level. The carbohydrate degradation also stops as energy is already provided by the external glucose.
Want to see more full solutions like this?
Chapter 47 Solutions
EBK LIFE: THE SCIENCE OF BIOLOGY
- If using animals in medical experiments could save human lives, is it ethical to do so? In your answer, apply at least one ethical theory in support of your position.arrow_forwardYou aim to test the hypothesis that the Tbx4 and Tbx5 genes inhibit each other's expression during limb development. With access to chicken embryos and viruses capable of overexpressing Tbx4 and Tbx5, describe an experiment to investigate whether these genes suppress each other's expression in the limb buds. What results would you expect if they do repress each other? What results would you expect if they do not repress each other?arrow_forwardYou decide to delete Fgf4 and Fgf8 specifically in the limb bud. Explain why you would not knock out these genes in the entire embryo instead.arrow_forward
- You implant an FGF10-coated bead into the anterior flank of a chicken embryo, directly below the level of the wing bud. What is the phenotype of the resulting ectopic limb? Briefly describe the expected expression domains of 1) Shh, 2) Tbx4, and 3) Tbx5 in the resulting ectopic limb bud.arrow_forwardDesign a grafting experiment to determine if limb mesoderm determines forelimb / hindlimb identity. Include the experiment, a control, and an interpretation in your answer.arrow_forwardThe Snapdragon is a popular garden flower that comes in a variety of colours, including red, yellow, and orange. The genotypes and associated phenotypes for some of these flowers are as follows: aabb: yellow AABB, AABb, AaBb, and AaBB: red AAbb and Aabb: orange aaBB: yellow aaBb: ? Based on this information, what would the phenotype of a Snapdragon with the genotype aaBb be and why? Question 21 options: orange because A is epistatic to B yellow because A is epistatic to B red because B is epistatic to A orange because B is epistatic to A red because A is epistatic to B yellow because B is epistatic to Aarrow_forward
- A sample of blood was taken from the above individual and prepared for haemoglobin analysis. However, when water was added the cells did not lyse and looked normal in size and shape. The technician suspected that they had may have made an error in the protocol – what is the most likely explanation? The cell membranes are more resistant than normal. An isotonic solution had been added instead of water. A solution of 0.1 M NaCl had been added instead of water. Not enough water had been added to the red blood cell pellet. The man had sickle-cell anaemia.arrow_forwardA sample of blood was taken from the above individual and prepared for haemoglobin analysis. However, when water was added the cells did not lyse and looked normal in size and shape. The technician suspected that they had may have made an error in the protocol – what is the most likely explanation? The cell membranes are more resistant than normal. An isotonic solution had been added instead of water. A solution of 0.1 M NaCl had been added instead of water. Not enough water had been added to the red blood cell pellet. The man had sickle-cell anaemia.arrow_forwardWith reference to their absorption spectra of the oxy haemoglobin intact line) and deoxyhemoglobin (broken line) shown in Figure 2 below, how would you best explain the reason why there are differences in the major peaks of the spectra? Figure 2. SPECTRA OF OXYGENATED AND DEOXYGENATED HAEMOGLOBIN OBTAINED WITH THE RECORDING SPECTROPHOTOMETER 1.4 Abs < 0.8 06 0.4 400 420 440 460 480 500 520 540 560 580 600 nm 1. The difference in the spectra is due to a pH change in the deoxy-haemoglobin due to uptake of CO2- 2. There is more oxygen-carrying plasma in the oxy-haemoglobin sample. 3. The change in Mr due to oxygen binding causes the oxy haemoglobin to have a higher absorbance peak. 4. Oxy-haemoglobin is contaminated by carbaminohemoglobin, and therefore has a higher absorbance peak 5. Oxy-haemoglobin absorbs more light of blue wavelengths and less of red wavelengths than deoxy-haemoglobinarrow_forward
- With reference to their absorption spectra of the oxy haemoglobin intact line) and deoxyhemoglobin (broken line) shown in Figure 2 below, how would you best explain the reason why there are differences in the major peaks of the spectra? Figure 2. SPECTRA OF OXYGENATED AND DEOXYGENATED HAEMOGLOBIN OBTAINED WITH THE RECORDING SPECTROPHOTOMETER 1.4 Abs < 0.8 06 0.4 400 420 440 460 480 500 520 540 560 580 600 nm 1. The difference in the spectra is due to a pH change in the deoxy-haemoglobin due to uptake of CO2- 2. There is more oxygen-carrying plasma in the oxy-haemoglobin sample. 3. The change in Mr due to oxygen binding causes the oxy haemoglobin to have a higher absorbance peak. 4. Oxy-haemoglobin is contaminated by carbaminohemoglobin, and therefore has a higher absorbance peak 5. Oxy-haemoglobin absorbs more light of blue wavelengths and less of red wavelengths than deoxy-haemoglobinarrow_forwardWhich ONE of the following is FALSE regarding haemoglobin? It has two alpha subunits and two beta subunits. The subunits are joined by disulphide bonds. Each subunit covalently binds a haem group. Conformational change in one subunit can be transmitted to another. There are many variant ("mutant") forms of haemoglobin that are not harmful.arrow_forwardWhich ONE of the following is FALSE regarding haemoglobin? It has two alpha subunits and two beta subunits. The subunits are joined by disulphide bonds. Each subunit covalently binds a haem group. Conformational change in one subunit can be transmitted to another. There are many variant ("mutant") forms of haemoglobin that are not harmful.arrow_forward
- Nutritional Sciences: From Fundamentals to Food, ...Health & NutritionISBN:9781337486415Author:McGuirePublisher:Cengage
- Biology 2eBiologyISBN:9781947172517Author:Matthew Douglas, Jung Choi, Mary Ann ClarkPublisher:OpenStax
