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PMID:16636458
| Citation |
Makino, Y and Omichi, K (2006) Purification of glycogen debranching enzyme from porcine brain: evidence for glycogen catabolism in the brain. Biosci. Biotechnol. Biochem. 70:907-15 |
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| Abstract |
Amylo-1,6-glucosidase from porcine brain was purified to homogeneity by ammonium sulfate fractionation, followed by sequential steps of liquid chromatography on DEAE-Sephacel, Sephacryl S-300, and Super Q. The purified enzyme had both maltooligosaccharide transferase and amylo-1,6-glucosidase activities within a single polypeptide chain, and the combination of these two activities removed the branches of phosphorylase limit dextrin. Based on these results, the purified enzyme was identified as a glycogen debranching enzyme (GDE). The molecular weight of the brain GDE was 170,000 by gel-filtration and 165,000 by reducing SDS-PAGE. The pH profile of maltooligosaccharide transferase activity coincided with that of the amylo-1,6-glucosidase activity (pH optimum at 6.0). The existence of GDE as well as glycogen phosphorylase in the brain explains brain glycogenolysis fully and supports the hypothesis that glycogen is a significant source of energy in this organ. |
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| Keywords |
Animals; Brain/enzymology; Chromatography, High Pressure Liquid; Glycogen/metabolism; Glycogen Debranching Enzyme System/isolation & purification; Glycogen Debranching Enzyme System/metabolism; Hydrogen-Ion Concentration; Swine |
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Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0004135: amylo-alpha-1,6-glucosidase activity |
ECO:0000314: |
F |
Fig. 3A |
complete | ||||
| GO:0004576: oligosaccharyl transferase activity |
ECO:0000314: |
F |
Fig. 4 |
complete | ||||
See also
References
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