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| Content Provider | PubMed Central |
|---|---|
| Author | Parker, David M. Alberto, Lodola Holbrook, J. John |
| Abstract | 1. The formation of the non-enzymic adduct of NAD+ and sulphite was investigated. In agreement with others we conclude that the dianion of sulphite adds to NAD+. 2. The formation of ternary complexes of either lactate dehydrogenase or malate dehydrogenase with NAD+ and sulphite was investigated. The u.v. spectrum of the NAD–sulphite adduct was the same whether free or enzyme-bound at either pH6 or pH8. This suggests that the free and enzyme-bound adducts have a similar electronic structure. 3. The effect of pH on the concentration of NAD–sulphite bound to both enzymes was measured in a new titration apparatus. Unlike the non-enzymic adduct (where the stability change with pH simply reflects HSO3 −=SO3 2−+H+), the enzyme-bound adduct showed a bell-shaped pH–stability curve, which indicated that an enzyme side chain of pK=6.2 must be protonated for the complex to form. Since the adduct does not bind to the enzyme when histidine-195 of lactate dehydrogenase is ethoxycarbonylated we conclude that the protein group involved is histidine-195. 4. The pH-dependence of the formation of a ternary complex of lactate dehydrogenase, NAD+ and oxalate suggested that an enzyme group is protonated when this complex forms. 5. The rate at which NAD+ binds to lactate dehydrogenase and malate dehydrogenase was measured by trapping the enzyme-bound NAD+ by rapid reaction with sulphite. The rate of NAD+ dissociation from the enzymes was calculated from the bimolecular association kinetic constant and from the equilibrium binding constant and was in both cases much faster than the forward V max.. No kinetic evidence was found that suggested that there were interactions between protein subunits on binding NAD+. |
| Starting Page | 959 |
| File Format | |
| ISSN | 14708728 |
| e-ISSN | 14708728 |
| Journal | Biochemical Journal |
| Issue Number | 3 |
| Volume Number | 173 |
| Language | English |
| Publisher Date | 1978-09-01 |
| Access Restriction | Open |
| Subject Keyword | Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Molecular Biology Biochemistry |
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