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stepladder [879]
2 years ago
11

Pepsin is a digestive enzyme. It is made in an inactive form, pepsinogen, which is activated by the acidity of the stomach to se

lf-cleave. The cleaved molecule is active pepsin, which goes on to cleave more pepsinogen molecules, leading to a cascade of rapid pepsin activation. This pathway is an example of________.
A. a positive feedback loop.
B. conditioning.
C. a negative feedback loop.
D. feedforward regulation.
E. homeostasis
Biology
2 answers:
grandymaker [24]2 years ago
5 0

Answer:

<h2>A</h2>

Explanation:

Pepsinogen is an inactive enzyme which is activated into active digestive enzyme known as pepsin. It is a digestive enzyme which causes breakdown of proteins. Active pepsin causes cleavage of more pepsinogen molecule by a positive feedback loop and leads to increase in the concentration of active pepsin molecule.

Its concentration increases according the requirement in the body which is controlled by feedback system.

Viktor [21]2 years ago
3 0
<h2>Option (A) is Right Answer</h2>

Explanation:

  (A) positive feedback loop

  • <em>Pepsin is a digestive enzyme</em>. It is made in a inactive structure, <em>pepsinogen</em>, which is enacted by the sharpness of the stomach to self-separate
  • The severed particle is dynamic <em>pepsin</em>, which proceeds to separate more pepsinogen atoms, prompting a course of fast pepsin enactment
  • Animals and population can keep up <em>homeostasis </em>in a domain when they have a consistent degree of births and passings. It is like the possibility of <em>harmony</em>
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Hi,

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Enolase is an enzyme that catalyzes one reaction in glycolysis in all organisms that carry out this process. The amino acid sequ
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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:

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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.

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