Abstract
1. 1. The aromatic circular dichroism of diphosphofructose phosphatase of the albino rat, golden Syrian hamster and New Zealand rabbit were used to compare their conformations. 2. 2. The conformational transitions incited by Na +, K +, pH, and spontaneous denaturation were compared and studied. 3. 3. From a comparative analysis of the tertiary structure of the phosphatases, as it is revealed by circular dichroism, it was concluded that the strong interactions of tyrosyl residues with non-polar micro-environments confer to the hamster enzyme a degree of rigidity which was found unmatched in the isofunctional protein of the rat.
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