摘要
在兔血小板膜中，血小板激活因子（ＰＡＦ）结合部位显示高度亲合性（Ｋｄ＝０．１±０．００７ｎｍｏｌ／Ｌ）、饱和性、显著的药理学特异性，其最大结合容量为２．８９±０．３２ｐｍｏｌ／ｍｇ蛋白。３Ｈ－ＰＡＦ饱和结合浓度为０．２ｎｍｏｌ／Ｌ。等温线表明为单一结合位点。红曲霉（Ｍｏｎａｓｃｕｓｓｐ．Ｆ４００）代谢产物中的小成份Ｄ（２Ａ）和Ｃ（４Ａ）与ＰＡＦ竞争受体结合部位，它们是ＰＡＦ的拮抗剂。Ｄ２Ａ的ＩＣ５０为３．１６×１０－５ｍｏｌ／Ｌ，Ｃ４Ａ的ＩＣ５０为３．０３×１０－５ｍｏｌ／Ｌ。
In rabbit platelet membrane 3H-PAF binding sites exhibited high affinity(Kd=0.1±0. 007nmol/L),saturability and marked pharmacological specificity, Themaximal binding capacity was 2.89±0.32pmol/mg protein.aturation of3H-PAF bindingwas obtained with 0. 2nmol/L ligand and its isotherm wf1s compatible with a single class ofbinding site. Two minor components (D2A and C4A)of the metabolites from Monascus sp.F400 inhibited the binding of PAF with the receptor.IC50 of D42A and C4A,were 3.16×10-5and 3.03×10-5mol/L respectively.
出处
《中国抗生素杂志》
CAS
CSCD
北大核心
1995年第5期321-324,共4页
Chinese Journal of Antibiotics
关键词
血小板激活因子
拮抗剂
解离常数
红曲霉
Platelet activating factor(PAF)
Platelet
Scatchard analysis
Dissociation constant
Monascus sp.
