大鼠血清磷酸胆碱结合蛋白与血小板活化因子之间的相互作用。
Interaction between rat serum phosphorylcholine binding protein and platelet activating factor.
作者信息
Randell E, Mookerjea S, Nagpurkar A
机构信息
Department of Biochemistry, Memorial University of Newfoundland St. John's, Canada.
出版信息
Biochem Biophys Res Commun. 1990 Mar 16;167(2):444-9. doi: 10.1016/0006-291x(90)92043-y.
The binding of rat serum phosphorylcholine binding protein (PCBP) to platelet activating factor (PAF) has been demonstrated using a HPLC-gel filtration technique. The bulk of the bound [3H]-PAF eluted with a higher molecular weight species of PCBP, possibly an aggregated form of PCBP. A smaller amount of [3H]-PAF co-eluted with the major monomeric species of PCBP. Formation of the PCBP-PAF complex was calcium dependent and could be inhibited by phosphorylcholine, suggesting the involvement of the phosphorylcholine binding site on PCBP. Binding of albumin and alpha 1-acid glycoprotein to PAF was not affected by phosphorylcholine or calcium. The specificity of this binding may explain the inhibitory effect of PCBP and related phosphorylcholine binding proteins on PAF induced aggregation of platelets.
已使用高效液相色谱 - 凝胶过滤技术证明大鼠血清磷酸胆碱结合蛋白（PCBP）与血小板活化因子（PAF）的结合。大部分结合的[³H] - PAF与较高分子量的PCBP一起洗脱，可能是PCBP的聚集形式。较少量的[³H] - PAF与PCBP的主要单体形式共洗脱。PCBP - PAF复合物的形成依赖于钙，并且可被磷酸胆碱抑制，这表明PCBP上的磷酸胆碱结合位点参与其中。白蛋白和α1 - 酸性糖蛋白与PAF的结合不受磷酸胆碱或钙的影响。这种结合的特异性可能解释了PCBP和相关磷酸胆碱结合蛋白对PAF诱导的血小板聚集的抑制作用。
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