Ostrich fructose-1,6-bisphosphatase: Kinetic characterization of the liver isoenzyme
✍ Scribed by André van Tonder; Ryno J. Naudé; Willem Oelofsen
- Publisher
- Elsevier Science
- Year
- 1991
- Tongue
- English
- Weight
- 568 KB
- Volume
- 23
- Category
- Article
- ISSN
- 0020-711X
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
Adsorption to blue dextran-Sepharose and successive elution with AMP and fructose 1,6-bisphosphate provides a one-step procedure for the simultaneous purification of fructose 1,6-bisphosphatase and fructose 1,Cbisphosphate aldolase from rabbit liver homogenates. The procedure can be completed in a s
## Abstract Using a streptozotocin‐induced type 1 diabetic rat model, we analyzed and separated the effects of hyperglycemia and hyperinsulinemia over the in vivo expression and subcellular localization of hepatic fructose 1,6‐bisphosphatase (FBPase) in the multicellular context of the liver. Our d
Both the synthesis and the degradation of Fru-2,6-P2 are catalyzed by a single enzyme protein; ie, the enzyme is bihnctional. This protein, which we have designated 6-phosphofructo 2-kinase/fructose 2,6-bisphosphatase is an important enzyme in the regulation of hepatic carbohydrate metabolism since