1983-01-01
Purification and properties of alanopine dehydrogenase isozymes from the channeled whelk, Busycotypus canaliculatum
Publication
Publication
Comparative Biochemistry and Physiology -- Part B: Biochemistry and
,
Volume 76
-
Issue 2
p. 321-
326
1. 1. Three tissue specific isozymes of alanopine dehydrogenase (ADH: alanopine: NAD oxidoreductase) were purified to homogeneity from foot muscle, gill and hepatopancreas of the channeled whelk, Busycotypus canaliculatum. 2. 2. Muscle ADH showed properties, in particular the effect of decreasing pH in lowering apparent Km's for pyruvate and l-alanine, which appear to gear this isozyme for alanopine synthesis as an end product of anaerobic glycolysis. 3. 3. The hepatopancreas isozyme, with a high affinity for meso-alanopine and NAD, appears suited for a role in alanopine oxidation in vivo. 4. 4. The properties of gill ADH are intermediate between those of the other two forms.
| Additional Metadata | |
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| Persistent URL | dx.doi.org/10.1016/0305-0491(83)90076-7 |
| Journal | Comparative Biochemistry and Physiology -- Part B: Biochemistry and |
| Citation |
Plaxton, W.C. (William C.), & Storey, K. (1983). Purification and properties of alanopine dehydrogenase isozymes from the channeled whelk, Busycotypus canaliculatum. Comparative Biochemistry and Physiology -- Part B: Biochemistry and, 76(2), 321–326. doi:10.1016/0305-0491(83)90076-7
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