Biología y Biomedicina >
Centro de Biología Molecular Severo Ochoa (CBM) >
(CBM) Artículos >
|Publisher:||American Society for Biochemistry and Molecular Biology|
|Citation:||The Journal of Biological Chemistry 17(2): 150-155 (1964)|
|Abstract:||Fructose-1, 6-diphosphatase (FDPase), a key enzyme in neoglycogenesis, is generally considered as essentially restricted to liver and kidney although a small activity had been early detected in skeletal muscle (Gomori 1943; Hers and Vanden Berghe 1957). Interest in the regulation of the activity of FDPase has been recently aroused by studies with liver and kidney preparations (Taketa and Pogell 1963; Mendicino and Vasarhely 1963; Krebs 1964 a; Newsholme 1963).
This communication reports the occurrence of significant amounts of FDPase in skeletal muscle of frog and rabbit. The frog muscle enzyme has a very great affinity for fructose-1, 6-P (FDP) as substrate and for AMP as allosteric inhibitor. The possible physiological significance of these kinetic properties and of the occurrence of this enzyme in muscle is discussed.|
|Publisher version (URL):||http://dx.doi.org/10.1016/0006-291X(64)90136-6|
|Appears in Collections:||(CBM) Artículos|
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.