Autor: |
E N, Zhmareva, G D, Zegzhda, G B, Kas'ian, O A, Livenskaia |
Rok vydání: |
1996 |
Předmět: |
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Zdroj: |
Ukrainskii biokhimicheskii zhurnal (1. 68(3) |
ISSN: |
0201-8470 |
Popis: |
Protein interaction with bioactive platinum and palladium complex compounds was studied by solid-phase sorbent assay (SSA), turbidimetry, isoelectric focusing and circular dichroism. In SSA reaction ability of metal compounds can be represented as follows: [equation: see text] Reaction ability of proteins can be represented as follows: hemoglobinserum albuminimmunoglobulin. The reaction products of serum albumin and metal compounds demonstrated more alkaline isoelectric points then the intact albumin resulting from adding positively charged metal centers [MeCl+, Me2+, [Me(H2O)n]2+, [Me(H2O)nCl]+ to albumin molecules. In metal-protein complexes circular dichroism demonstrated the diminution of alpha-helix structure percentage if compared with intact albumin, the most prominent effect being caused by K2[PdCl]4. The conformational distortion of albumin was significant. Metal compounds mostly affected the optical activity of S-S-protein bands (251-254 nm). Experimental evidence confirmed the hypothesis that platinum metal complexes with high reaction ability are less toxic than those with low reaction ability. |
Databáze: |
OpenAIRE |
Externí odkaz: |
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