[Interaction of proteins with platinum and palladium compounds with differing biological activities].
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: hemoglobin > serum albumin > immunoglobulin. 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.
Zhmareva
E N
EN
Zegzhda
G D
GD
Kas'ian
G B
GB
Livenskaia
O A
OA
D000818:Animals; D002942:Circular Dichroism; D006454:Hemoglobins / Q000378:metabolism*; D006736:Horses; D006801:Humans; D007136:Immunoglobulins / Q000378:metabolism*; D007526:Isoelectric Point; D009391:Nephelometry and Turbidimetry; D010165:Palladium / Q000378:metabolism* / Q000494:pharmacology; D017671:Platinum Compounds / Q000378:metabolism* / Q000494:pharmacology; D012709:Serum Albumin / Q000378:metabolism*; D013056:Spectrophotometry, Ultraviolet
D006454:Hemoglobins; D007136:Immunoglobulins; D017671:Platinum Compounds; D012709:Serum Albumin; D010165:Palladium