Abstract
1. 1. Brook trout hexose-6-phosphate dehydrogenase (H6PD) and lake trout H6PD are essentially identical in several parameters including pH optima, kinetic properties and activation energy. They differ in thermal stability. 2. 2. The various oxidations catalyzed by trout H6PD differ in their response to the presence of Mg2+, ATP and several anions. 3. 3. The apparent Km's of all four substrates show a decrease with decreasing temperature. 4. 4. Kinetics of substrate oxidation by H6PD suggest that the enzyme most likely functions as a G6PD.
Original language | English (US) |
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Pages (from-to) | 241-256 |
Number of pages | 16 |
Journal | Comparative Biochemistry and Physiology -- Part B: Biochemistry and |
Volume | 43 |
Issue number | 2 |
DOIs | |
State | Published - Oct 15 1972 |
Keywords
- ATP
- Glucose-6-phosphate dehydrogenase
- Mg
- Salvelinus fontinalis
- Salvelinus namaycush
- acclimation
- activation energy
- anions
- brook trout
- enzyme inhibition
- enzyme kinetics
- enzyme stimulation
- hexose-6-phosphate dehydrogenase
- isoelectric point
- lake trout
- pH optima
- salmonids
- thermal denaturation
ASJC Scopus subject areas
- Biochemistry
- Physiology
- Molecular Biology