Answer:
B) rough ER → Golgi complex → Golgi vesicle → extracellular fluid
Explanation:
- Insulin is synhtesized by beta cells of pancereas (preproinsulin).
- Insulin enters the rough endoplasmic reticulumn in its inactive form (proinsulin).
- The rough endoplasmic reticulumn converts it to active form (insulin).
- The rough endoplasmic reticulumn transfer the insulin to glogi comlpex
- The Golgi complex secrete it in golgi vesicles to cytoplasm.
- On the stimulation of beta cells insulin is secreted to extracellular fluid..
C is incorrect
Both acids and bases produce ions in solution, are electrolytes, and conduct electricity in solution. Although red litmus is an indicator, it does not change color in an acid, acids are proton donors while bases are proton acceptors. Soaps often contain bases, not acids.
D) conduct electricity in water. is the correct answer
The correct term to fill in the blank would be intensity. The intensity of exercise determines whether carbohydrates or fat is the predominant source of energy production. During high-intensity workouts, it is the fat that is used as the source of energy production while low-intensity exercises would only use the carbohydrates present for energy.
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.
