Investigation of some physico-chemical properties of muscular parvalbumins by means of the luminescence of their phenylalanyl residues.
Biochim Biophys Acta, 1975/7/21;400(1):1-16.
Burstein EA, Permyakov EA, Emelyanenko VI, Bushueva, Pechère JF
PMID: 238652
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.
MeSH terms
Albumins; Animals; Binding Sites; Calcium; Carps; Egtazic Acid; Fishes; Hydrogen-Ion Concentration; Kinetics; Luminescent Measurements; Mathematics; Muscle Proteins; Muscles; Phenylalanine; Protein Binding; Protein Conformation; Protein Denaturation; Spectrometry, Fluorescence; Temperature
More resources
EndNote: Download