Synthesis and characterization of soluble dextran-adenosine phosphate complexes: kinetic effects of coenzyme loading.
Soluble dextran-ATP complexes have been synthesized using a bifunctional oxirane as the coupling agent. The degree of coupling is time-dependent, allowing materials of varying coenzyme loadings to be produced very simply. Characterization studies have shown that at the maximum coenzyme loading obtained (34 molecules per complex) all coenzyme moieties were coenzymically active with hexokinase. The extent of coenzyme loading was shown to have a considerable influence on the values of Km and Vmax of the complex as a substrate for hexokinase. Enzyme activity was also found with acetate kinase and myokinase, and coenzyme recycling (ATP, ADP) was demonstrated in an ultrafiltration reactor.
School of Chemical Engineering, University of Bath, UK.
J
J
Hubble
R
R
Eisenthal
A
A
Herbert
I
I
Tarr
R
R
England
D000084:Acetate Kinase / Q000378:metabolism; D000244:Adenosine Diphosphate / Q000138:chemical synthesis*; D000255:Adenosine Triphosphate / Q000138:chemical synthesis*; D000263:Adenylate Kinase / Q000378:metabolism; D003067:Coenzymes; D003911:Dextrans / Q000138:chemical synthesis*; D006593:Hexokinase / Q000378:metabolism; D007202:Indicators and Reagents; D007700:Kinetics; D013379:Substrate Specificity
D003067:Coenzymes; D003911:Dextrans; D007202:Indicators and Reagents; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D006593:Hexokinase; D000084:Acetate Kinase; D000263:Adenylate Kinase