Protein-Metal ion interaction: volume effects produced by the interaction of proteins with metal ions
| Autor: | Linda Carol Roberson, Sam Katz |
|---|---|
| Rok vydání: | 1976 |
| Předmět: |
chemistry.chemical_classification
biology Chemistry Globular protein Metal ions in aqueous solution Albumin Proteins General Medicine Biochemistry Metal Structure-Activity Relationship Crystallography chemistry.chemical_compound Volume (thermodynamics) Myoglobin Metals Cations visual_art biology.protein visual_art.visual_art_medium Bovine serum albumin Lysozyme Protein Binding Nuclear chemistry |
| Zdroj: | Bioinorganic Chemistry. 6:143-154 |
| ISSN: | 0006-3061 |
| DOI: | 10.1016/s0006-3061(00)80211-2 |
| Popis: | The interaction of metal cations with single chain globular proteins produces volume increases, the magnitude of which is determined primarily by the ion and to a lesser extent by the protein. The cations are listed in ascending order of volume change: K(I) less than Mg(II) less than Sr(II) less than Ca(II) less than Co(II) less than Ni(II) less than Cd(II) less than Zn(II) less than Cu(II) less than Pb(II). This sequence held for all cation-protein systems investigated except for Cd(II) which produced a slightly larger volume effect than Zn(II) with lysozyme. The volume changes attributed to protein-cation interaction are positive and range from 8 ml/10(5) g of protein for the reaction on 0.05 M KNO3 with bovine plasma albumin to 2320 ml/10(5) g of protein produced by the 0.20 M Pb(NO3)2-myoglobin system. A similar classification scheme was not possible for the proteins. For example, volume increases of 45, 50, 80 and 95 ml/10(5) g of protein were produced when 0.05 M Mg(II) reacted with bovine serum albumin, ovalbumin, sperm whale myoglobin and lysozyme, respectively. However, when 0.2 M Pb(II) was the reactant the values were 1930, 846, 2320, and 1120 ml/10(5) g of protein. Volume effects produced by Cr(III), Al(III) and Fe(III) were determined, but the calculated results are considered dubious because the volume changes are a complicated function of protein-cation and protein-proton interaction. |
| Databáze: | OpenAIRE |
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