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- W1489376146 abstract "Abstract To determine whether equilibrium binding between and hepatocytes involves a cell surface receptor for albumin, we incubated freshly isolated rat hepatocytes with 125I-albumin and determined the amount of associated with the cells as a function of the total concentration. The resulting two-phase binding curve showed the rat albumin-hepatocyte interaction to consist of a saturable binding interaction with a dissociation constant of 1.1 microM and 2 X 10(6) sites/cell in addition to a weak, nonsaturable binding interaction. However, the saturable binding of to hepatocytes did not appear to result from the presence of an receptor on the cell surface; the interaction was the same for different species of albumin, for chemically modified albumins, and for fragments of representing mutually exclusive domains of the molecule. The saturable binding was, instead, found to involve a subpopulation of with an enhanced affinity for the cell surface. We show that this subpopulation of is generated upon contact with either solid surfaces or cell surfaces and can be transferred from one surface to another. We propose that the two-phase Scatchard binding curve and the albumin receptor effect reflect two populations of that bind to the cell surface with different affinities rather than one population of that binds to two classes of binding sites." @default.
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- W1489376146 date "1989-06-01" @default.
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- W1489376146 title "The albumin receptor effect may be due to a surface-induced conformational change in albumin" @default.
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- W1489376146 doi "https://doi.org/10.1016/s0021-9258(18)81738-0" @default.
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