Abstract
Summary
Glyceraldehyde-3-phosphate dehydrogenase has been purified from rainbow trout acclimated to 15° (warm) and 5° (cold) and compared with respect to their electrophoretic properties, NAD-binding behavior, and ultraviolet absorption. Both the warm and cold species of G3PDH show the same electrophoretic properties. They differ, however, in NAD-binding behavior and in ultraviolet-absorption properties. It was concluded that temperature acclimation brings about a conformational change in the higher-order structure of G3PDH which is stable through purification procedures.
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