Abstract
The drug-binding properties of human alpha-foetoprotein (alpha FP) were investigated by a fluorescence-spectral method. Human alpha FP was shown to bind to albumin's site I marker (warfarin, phenylbutazone), site II marker (L-tryptophan), but not site III marker (cholic acid, digoxin). The binding of human alpha FP towards lower alcohols was examined, and this binding seems to depend partly on the hydrophobicity of the ligands. The binding of human alpha FP is discussed in comparison with human serum albumin or rat alpha FP.
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Selected References
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