Investigation of some physico-chemical properties of muscular parvalbumins by means of the luminescence of their phenylalanyl residues
| Autor: | Edward A. Burstein, Victor I. Emelyanenko, Eugene A. Permyakov, Jean-François Pechere, T.L. Bushueva |
|---|---|
| Rok vydání: | 1975 |
| Předmět: |
Protein Denaturation
Conformational change Carps Protein Conformation Phenylalanine Parvalbumins Inorganic chemistry Muscle Proteins Biochemistry Genetics and Molecular Biology (miscellaneous) chemistry.chemical_compound Albumins Animals Organic chemistry Carp Egtazic Acid Binding Sites biology Chemistry Muscles Fishes Temperature Hydrogen-Ion Concentration Chromophore biology.organism_classification Fluorescence Kinetics EGTA Spectrometry Fluorescence Luminescent Measurements Calcium Luminescence Mathematics Protein Binding |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Protein Structure. 400:1-16 |
| ISSN: | 0005-2795 |
| DOI: | 10.1016/0005-2795(75)90121-x |
| Popis: | The influence of pH, temperature and Ca2+-release on the phenylalanyl and tyrosyl fluorescence 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|