glycogen phosphorylase

After all this is done, glycogen phosphorylase can continue.

Myophosphorylase is the form of the glycogen phosphorylase found in muscle.

This change was shown to correlate to an activity increase for liver glycogen phosphorylase.

Glycogen phosphorylase was the first allosteric enzyme to be discovered.

The inhibition of glycogen phosphorylase has been proposed as one method for treating type 2 diabetes.

Glycogen can change into glucose 6-phosphate as well with the help of glycogen phosphorylase.

Returning to glycogen phosphorylase, the less active "b" form can itself be activated without the conformational change.

Glycogen phosphorylase is regulated by both allosteric control and by phosphorylation.

New markers such as glycogen phosphorylase isoenzyme BB are under investigation.

This amplifies the effect of activating glycogen phosphorylase.

They seem not to have glycogen phosphorylase, which is present in astrocytes to degrade glycogen.

Glycogen phosphorylase is the primary enzyme of glycogen breakdown.

In mammals, the major isozymes of glycogen phosphorylase are found in muscle, liver, and brain.

Also, vitamin B is a required coenzyme of glycogen phosphorylase, the enzyme necessary for glycogenolysis to occur.

A number of incremental but important discoveries through the 1950s added to their research, primarily focusing on the activity of glycogen phosphorylase in dog liver.

Glycogen phosphorylase breaks up glycogen into glucose subunits.

Glycogen phosphorylase can act only on linear chains of glycogen (α1-4 glycosidic linkage).

The final, perhaps most curious site on the glycogen phosphorylase protein is the so-called glycogen storage site.

Glycogen is broken down rapidly via glycogen phosphorylase into individual glucose units during intense exercise.

AMP activates glycogen phosphorylase b by changing its conformation from a tense to a relaxed form.

Epinephrine not only activates glycogen phosphorylase but also inhibits glycogen synthase.

The increased calcium availability binds to the calmodulin subunit and activates glycogen phosphorylase kinase.

This activates glycogen phosphorylase and inhibits glycogen synthase.

Glycogen phosphorylase catalyzes the first step in glycogenolysis, the process of breaking glycogen into its substituent glucose parts.

Hormones such as epinephrine, insulin and glucagon regulate glycogen phosphorylase using second messenger amplification systems that are linked to G proteins.