Glycogen phosphorylase is one of the phosphorylase enzymes (EC2.4.1.1). It breaks up glycogen into glucose subunits. Glycogen is left with one less glucose molecule, and the free glucose molecule is in the form of glucose-1- phosphate. In order to be used for metabolism, it must be converted to glucose-6-phosphate by the enzyme phosphoglucomutase. Glycogen phosphorylase can only act on linear chains of glycogen (aa1-4 glycosidic linkage). Its work will immediately come to a halt four residues away from a 1-6 branch (which are exceedingly common in glycogen). In these situations, a debranching enzyme is necessary, this will straighten out the chain in that area. Additionally, an alpha 1-6 glucosidase enzyme is required to break the remaining 1-6 residue that remains in the new linear chain. After all this is done, glycogen phosphorylase can continue. An insulin stimulated enzyme known as phosphoprotein phosphatase (PP-1) inactivates glycogen phosphorylase to prevent glycogen break up. GPBB - a sensitive marker for the AMI diagnosis within 4 hours after the onset of chest pain. It has also been shown that GPBB is increased in a considerable proportion of AMI patients within 2-3 hours from chest pain onset. GPBB is increased early in patients with unstable angina. GPBB can also be a sensitive marker for the detection of peri-operative myocardial ischaemia and infarction in patients undergoing coronary artery bypass grafting.
Source:Recombinant protein corresponding to human Glycogen Phosphorylase, a single, non- glycosylated, polypeptide chain, expressed in E. coli.
Molecular Weight:~97kD
Applications:Suitable for use in Immunoassays and Western Blot. Other applications not tested.
Recommended Dilution:Optimal dilutions to be determined by the researcher.
Storage and Stability:May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
