In an experiment to test the role of glycogen phosphorylase during exercise, you

Question

In an experiment to test the role of glycogen phosphorylase during exercise, you generate a mutant strain of mice that has very low levels of active glycogen phosphorylase enzyme. These mice are subjected to intense, anaerobic exercise for varying periods of time. During this exercise period, blood is withdrawn every few minutes and tested for lactate. Samples from mutant mice are compared with control samples from wild-type mice (that have normal glycogen phosphorylase). The results are shown in the graph above.

********************Why isn't there an increase in the blood lactate concentration in the mutant mouse?

I know that the mutant mouse has no increase in blood lactate concentration because it has the low levels of the glycogen phosphorylase enzyme. In animals, glycogen is broken down through the enzyme glycogen phosphorylase, which catalyzes an attack by Pi on the ?1?4 glycosidic linkage. So does that simply mean that lacking the enzyme will "block" the breakdown of glycogen into glucose and prevents the formation of lactic acid?

Explanation / Answer

Answer:

The graph with time in minutes on the X-axis and concentration of blood lactose (mg/100ml) on Y-axis. The results of the two strains, one is mutant and other is wild type, are shown in the graph. The results from the graph shows that mutant did not show any increase of decrease in the blood lactose concentrations, indicating that mutant did not have enzyme glycogen phosphorylase.

The wild strains shows high or maximum blood lactose concentrations at 5min time(60 mg/100ml) and then decreased to 35 mg/100ml at 10 min time. further decrease to 25 mg/100ml is observed at 25 min time. the increase in blood lactose is due to presence of enzyme glycogen phosphorylase

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