@article{0c31b1930253468497c893629c025211,
title = "Coenzyme binding, observed by fluorescence enhancement, apparently unrelated to the enzymic activity of glutamic dehydrogenase",
author = "Carl Frieden",
note = "Funding Information: ment observed in experiments similar to that shown in Fig. I and which has been observed by others 4 is a result of TPNH binding to a site which is not catalytically active in the sense that it determines the kinetic parameters of the reaction. What the function of this site, which incidentally binds DPNH as well as TPNH, may be is not yet known. The occurrence of the two types of sites described above explains the discrepancies noted between the kinetic and fluorimetric data. It should be pointed out that glutamic dehydrogenase is not the only case where such discrepancies have been observed. SCHWERT has found differences up to io-fold for the DPNH binding to lactic dehydrogenase 8 and VELICK et al.S, 9 have observed a binding constant for DPN binding to 3-phosphoglyceraldehyde dehydrogenase much smaller than the previously published kinetic constant indicated 1°. In fact, the differences between the kinetic and fluorimetric binding constant may be as large as IOOO-foldn . It is tentatively suggested that for these enzymes, the binding of coenzyme observed in the fluorimetric titrations does not represent binding to the coenzyme site which determines the kinetic parameters. Further work is in progress on this problem and more complete details will appear elsewhere. This work was supported by a research grant, No. R.G. 5704, from the National Institutes of Health, U.S. Public Health Service.",
year = "1961",
month = feb,
day = "18",
doi = "10.1016/0006-3002(61)90316-X",
language = "English",
volume = "47",
pages = "428--430",
journal = "BBA - Biochimica et Biophysica Acta",
issn = "0006-3002",
number = "2",
}