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- W2079832564 abstract "The influence of pH, temperature and Ca2+-release on the phenylalanyl and tyrosyl fluorescene of muscular parvalbumins from white muscles of hake and carp has been investigated. Within the pH range from 7 to 8, Ca2+-saturated parvalbumins show a conformational change registered by fluorescence, that is associated with the release of some of the bound Ca2+. Removal of Ca2+ by means of EGTA (ethyleneglycolbis-(aminoethylether)tetra-acetic acid) considerably narrows the region of protein nativity, increases the accessibility of their chromophores to quencher ions (Cs+ and CNS-) and decreases their stability against heat denaturation. The usefulness of measurements of the phenylalanine fluorescence and of the tyrosine-phenylalanine energy transfer in the investigation of these and other proteins is discussed." @default.
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- W2079832564 date "1975-07-01" @default.
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- W2079832564 title "Investigation of some physico-chemical properties of muscular parvalbumins by means of the luminescence of their phenylalanyl residues" @default.
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- W2079832564 doi "https://doi.org/10.1016/0005-2795(75)90121-x" @default.
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