人甲胎蛋白的药物结合特性
Drug-binding properties of human alpha-foetoprotein.
作者信息
Hirano K, Watanabe Y, Adachi T, Ito Y, Sugiura M
出版信息
Biochem J. 1985 Oct 1;231(1):189-91. doi: 10.1042/bj2310189.
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.
摘要
采用荧光光谱法研究了人甲胎蛋白（αFP）的药物结合特性。结果表明，人αFP可与人血清白蛋白的位点I标记物（华法林、保泰松）、位点II标记物（L-色氨酸）结合，但不与位点III标记物（胆酸、地高辛）结合。研究了人αFP与低级醇的结合情况，这种结合似乎部分取决于配体的疏水性。将人αFP的结合情况与人血清白蛋白或大鼠αFP进行了比较讨论。
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