A test of biochemical symmorphosis in a heterothermic tissue: bluefin tuna white muscle.

Abstract

To test predictions of biochemical symmorphosis, we measured the activity of seven consecutive glycolytic enzymes at three positions along the heterothermic white muscle of the bluefin tuna. Biochemical symmorphosis predicts that adjustments in sequential enzyme concentrations along a thermal gradient should occur as a function of the thermal sensitivity of the enzymes to ensure that no one enzyme in the pathway is in excess at any point along the gradient. We found no evidence for adjustments in enzyme quantity or quality along the thermal gradient, as well as no evidence for the prediction that the more temperature-sensitive enzymes would exhibit more dramatic compensation. Conservation of glycolytic flux in the cold exterior and warm interior muscle may be achieved by the near insensitivity of glyceraldehyde-3-phosphate dehydrogenase to temperature in this tissue. This may have the added benefit of moderating flux during seasonal or transient changes in the thermal gradient. According to the strictest application of biochemical symmorphosis, such a mechanism represents adequate, yet suboptimal design.