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- W2036734914 abstract "The effects of protein concentration, alkaline pH and specific bound ligands on the reversibility of thermal denaturation of Delphinus delphis myoglobin have been studied. Denaturation has been followed by absorption changes in the Soret band. It was established experimentally that by lowering the protein concentration below 1 · 10−5 M at pH 9.0 a decrease in the degree of renaturation was obtained for the three ferrimyoglobin derivatives studied. It is shown that reversibility depended strongly on the ionization of the amino acid residues lying on the surface of the protein molecule and probably associated in “cluster groups”. These probably are: (a) 6 lysyl groups titrated in the region pH 9.5–10.2; (b) the distal histidine (E7), depending on the nature of the sixth haem ligand; (c) the abnormally titrated tyrosine (H23). Reversibility was definitely influenced by the nature of the ligands in two ways, namely by their effect on the conformational stability of the molecule and on the stability of the hydrogen bonding between the ligand and the distal histidine. The specific effect of tyrosyl groups on the mechanism of reversibility is discussed. Total renaturation of cyanide ferrimyoglobin at pH 9.5 was shown and conditions for it were selected on the basis of these studies." @default.
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- W2036734914 date "1970-07-01" @default.
- W2036734914 modified "2023-10-18" @default.
- W2036734914 title "On the reversibility of thermal denaturation of Delphinus delphis ferrimyoglobin derivatives" @default.
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- W2036734914 doi "https://doi.org/10.1016/0005-2795(70)90071-1" @default.
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