[Molecular aspects of the interaction between albumin and tannin-treated erythrocytes in the process of hemosensitization. Report 1. Stable and unstable effects. Quantitative parameters].
A study was made of the process of interaction between the tannin-treated sheep erythrocytes and the human serum albumin. Protein binding increased, whereas the loose/stable binding ratio decreased with the rise of the initial protein concentration. The process of stable albumin binding is described by the Langmour equation, this permitting to assess the limiting binding values -- about 6-10(5) molecules per erythrocyte. Albumin molecules were bound by erythrocyte with their greatest surface. At any concentration albumin was incapable of occupying more than 85% of the erythrocyte surface; at 90% binding level it blocked only 51--52% of the tannin-treated erythrocyte. The data obtained were regarded as a methodical basis for the preparation of erythrocytic diagnostic agents with the proteins of albumin type.
D000818:Animals; D006386:Hemagglutination Tests; D006801:Humans; D011485:Protein Binding; D012709:Serum Albumin / Q000276:immunology*; D012756:Sheep; D013634:Tannins
D012709:Serum Albumin; D013634:Tannins
Molekuliarnye aspekty vzaimodeĭstviia al'bumina i tanizirovannykh éritrotsitov v protsesse gemosensibilizatsii. Soobshchenie 1. Prochnoe i rykhloe deĭstvie. Kolichestvennye parametry