منابع مشابه
Kinetic mechanism of potato phosphorylase.
Polysaccharide phosphorylase isolated from Idaho potatoes was the subject of a steady state kinetic study. The initial velocity of the reaction between a-D-glucopyranose l-phosphate (glucose-l-P) and amylopectin, in the absence of orthophosphate, was determined as a function of substrate concentration. A similar study was carried out for the reverse reaction. The result is characteristic of a s...
متن کاملKinetic mechanism of phosphorylase b. Rates of initial velocities and of isotope exchange at equilibrium.
In order to assign a kinetic mechanism to phosphorylase b, initial rate studies were conducted in conjunction with isotope exchange studies at equilibrium. Initial velocity rates were measured with varied concentrations of both substrates in each direction, in the presence of saturating levels of AMP. Data were analyzed with double reciprocal plots and secondary replots of intercepts and slopes...
متن کاملKinetic mechanism of rabbit muscle glycogen phosphorylase a.
Isotope-exchange rates at chemical equilibrium were determined for the glycogen-a-D-glucopyranose l-phosphatePi system in the presence of phosphorylase a. Exchange of 32P from a-n-glucopyranose l-phosphate (glucose-l-P) into Pi and exchange of 14C from glucose-l-P into glycogen were followed simultaneously by the use of glucose-l-P containing both isotopes. Concentrations of glucose-l-P and Pi ...
متن کاملORDERED MECHANISM OF BINDING OF PHOSPHORYLASE KINASE AND GLYCOGEN PHOSPHORYLASE b TO GLYCOGEN
The kinetics of the interaction of rabbit skeletal muscle phosphorylase kinase with glycogen has been studied using turbidimetric method (40 mM Hepes, pH 6.8, and 8.2; 20◦C). The binding of phosphorylase kinase with glycogen occurs only in the presence of Ca and Mg . According to the kinetic data, phosphorylase b favors the binding of phosphorylase kinase with glycogen. This conclusion is suppo...
متن کاملPurine nucleoside phosphorylase. Kinetic mechanism of the enzyme from calf spleen.
Ribose 1-phosphate, phosphate, and acyclovir diphosphate quenched the fluorescence of purine nucleoside phosphorylase at pH 7.1 and 25 degrees C. The fluorescence of enzyme-bound guanine was similar to that of anionic guanine in ethanol. Guanine and ribose 1-phosphate bound to free enzyme, whereas inosine and guanosine were not bound to free enzyme in the absence of phosphate. Thus, synthesis p...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1969
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)63562-8