Abstract

1. 1. The nanomolar level of activity for phosphofructokinase suggests that it functions as a rate-limiting enzyme. 2. 2. The high triosephosphate isomerase and glyceraldehyde-3-phosphate dehydrogenase activities suggest that their role is in lipid synthesis and degradation. 3. 3. The comparatively high hexokinase activity and activities of triosephosphate isomerase, glyceraldehyde-3-phosphate dehydrogenase, enolase and pyruvate kinase propose a discontinuous glycolytic pathway. 4. 4. The activities of these enzymes indicate that the glycolytic capacity of Luidia clathrata is lower than other invertebrate digestive and muscle tissues.

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