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- W1546779174 abstract "Abstract 1. 1. Significant and specific changes in the aromatic circular dichroic spectrum of liver diphosphofructose phosphatase result upon binding of the substrate, fructose 1,6 diphosphate, of the inhibitor, 5'AMP, and of an activator, (ethylenedinitrilo)tetraacetate (EDTA). Such conformational transitions are of identical nature in the rat and hamster enzyme. However, the phosphatase derived from the rat exhibits a greater susceptibility to conformational transitions. 2. 2. The conformational transitions incited upon binding of 5'AMP are revealed primarily by a large increase in the rigidity of certain phenylalanyl residues. 3. 3. Substrate binding incites an alteration of the assymetric environment of certain tyrosyl residues. 4. 4. The activation of the enzyme by EDTA appears to be associated with an overall decrease in the rigidity of the protein molecule, an effect similar to that induced at alkali solution." @default.
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- W1546779174 date "1976-01-01" @default.
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- W1546779174 title "Exploitable molecular mechanisms in hibernation—III" @default.
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- W1546779174 doi "https://doi.org/10.1016/0020-711x(76)90069-0" @default.
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