Abstract
ApoGPDH is shown to exhibit half-of-the-sites reactivity towards iodeacetamido-naphthal (IAN) and FDNB and all-of-the-sites reactivity towards DTNB, iodoactic acid and the large DDPM molecule. It is suggested that the asymmetry in the ApoGPDH molecule is induced by some alkylating reagents and not by others, depending on the nature of the interaction between the alkyl group and the active site of the enzyme.
| Original language | English |
|---|---|
| Pages (from-to) | 889-893 |
| Number of pages | 5 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 54 |
| Issue number | 3 |
| DOIs | |
| State | Published - 1 Oct 1973 |
| Externally published | Yes |
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