Lipoamide dehyrogenase immobilized on porous glass.
Lipoamide dehydrogenase (NADH:lipoamide oxidoreductase, EC 22.214.171.124) isolate from pig heart and Escherichia coli was covalently coupled by both diazonium and amide bonds to controlled pore glass beads (96% silica). When the enzyme was immobilized in the presence of NAD+, the enzyme no longer exhibited its normal requirement for NAD+ for full activity. If the immobilized enzyme was then treated with NADase, the requirement for NAD+ was restored. Enzyme immobilized in the absence of NAD+ exhibited normal NAD+ dependence both prior to an after NADase treatment. These results are discussed in terms of co-immobilization of NAD+ at or near the allosteric site of the enzyme.
Published In/Presented At
Scouten, W. H., Knowles, H., Jr, Freitag, L. C., & Iobst, W. (1977). Lipoamide dehyrogenase immobilized on porous glass. Biochimica et biophysica acta, 482(1), 11–18. https://doi.org/10.1016/0005-2744(77)90348-5
Medicine and Health Sciences
Department of Medicine