The following are the steps the nurse would take to treat the infiltrated site:
1. Stop the infusion and remove the catheter
2. Elevate the extremity
3. Encourage an active range of motion
4. Apply a cold or warm compress depending on the solution infusing
5. Restart the infusion proximal to the location or in another extremity
Now, in order to address hydration requirements of the client, the nurse will have to begin a novel peripheral intravenous in another extremity or to again start the infusion if intravenous access has been created.
Some of those lysosomes contain secretions that will help the immune cells destroy foreign pathogens.
Hope that helped you.
A scientist must always try to avoid bias in scientific
experiments. It is important for scientist to avoid leaning into their bias
when trying to confirm their hypothesis. As much as possible the scientist
should be able to follow the scientific method to avoid bias.
Answer:
a) The response indicates that a pH below or above this range will most likely cause enolase to denature/change its shape and be less efficient or unable to catalyze the reaction.
b)The response indicates that the appropriate negative control is to measure the reaction rate (at the varying substrate concentrations) without any enzyme present.
c)The response indicated that the enolase has a more stable/functional/correct/normal protein structure at the higher temperature of 55°C than at 37°C because the enzyme is from an organism that is adapted to growth at 55°C.
Explanation:
Enolase catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate during both glycolysis and gluconeogenesis.In bacteria, enolases are highly conserved enzymes and commonly exist as homodimers.
The temperature optimum for enolase catalysis was 80°C, close to the measured thermal stability of the protein which was determined to be 75°C, while the pH optimum for enzyme activity was 6.5. The specific activities of purified enolase determined at 25 and 80°C were 147 and 300 U mg−1 of protein, respectively. Km values for the 2-phosphoglycerate/phosphoenolpyruvate reaction determined at 25 and 80°C were 0.16 and 0.03 mM, respectively. The Km values for Mg2+ binding at these temperatures were 2.5 and 1.9 mM, respectively.
Enolase-1 from Chloroflexus aurantiacus (EnoCa), a thermophilic green non-sulfur bacterium that grows photosynthetically under anaerobic conditions. The biochemical and structural properties of enolase from C. aurantiacus are consistent with this being thermally adapted.
