Immobilized triosephosphate isomerases. A comparative study.
Pig muscle triosephosphate isomerase was covalently attached to polyacrylamide and silica-based supports possessing carboxylic or aldehyde functional groups or activated with p-benzoquinone. A silica-based support activated with p-benzoquinone proved to be the most advantageous. There were no profound alterations in the catalytic properties as a result of the immobilization. The immobilization enhanced the resistance against urea and heat treatment. At the start of the treatments, the enzyme was activated. The extent of activation depended on the pH, and on the buffer and salt concentrations. Increase of the ionic strength decreased or eliminated the activation. The phosphate ion had a specific effect on the thermal inactivation.
Abrahám
M
M
Department of Biochemistry, Atilla József University, Szeged, Hungary.
Alexin
A
A
Szajáni
B
B
D000818:Animals; D001709:Biotechnology; D004789:Enzyme Activation; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000037:antagonists & inhibitors / Q000378:metabolism*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D009132:Muscles / Q000201:enzymology; D013552:Swine; D014305:Triose-Phosphate Isomerase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D014508:Urea / Q000494:pharmacology
D004800:Enzymes, Immobilized; D014508:Urea; D014305:Triose-Phosphate Isomerase