...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Biochemistry >MULTIPLE BINDING WITH IDENTICAL LINKAGE - A MECHANISM THAT EXPLAINS THE EFFECT OF LIPOPROTEIN(A) ON FIBRINOLYSIS
【24h】

MULTIPLE BINDING WITH IDENTICAL LINKAGE - A MECHANISM THAT EXPLAINS THE EFFECT OF LIPOPROTEIN(A) ON FIBRINOLYSIS

机译：多重结合与同构联结-解释脂蛋白（A）对纤维蛋白溶解作用的机制

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

We have previously shown that both recombinant apo(a) and native Lp(a) inhibit the binding of Glu-plasminogen to fibrin surfaces [Fleury & Angles-Cano (1991) Biochemistry 30, 7630-7638; Rouy et al. (1992) Biochemistry 31, 6332-6339]. The aim of the present study was to characterize the mechanism of this inhibition and to define the parameters governing binding when two different Lp(a) species compete with plasminogen for fibrin, a situation that may be found in vivo in subjects heterozygous for the apo(a) trait. The K-d for the binding of plasminogen to fibrin was 660 nM whereas the affinity of Lp(a) was inversely related to apo(a) size (K-d range: 50 to >500 nM). To determine the effect of plasminogen on Lp(a) binding and reciprocally, competition experiments were performed. The K-d of either Lp(a) or plasminogen for fibrin remained unchanged in the presence of the other competitor whereas B-max, the maximal amount bound, was importantly decreased. In a similar fashion, competition for fibrin binding among Lp(a) isoforms was shown with the use of Lp(a) density fractions containing varying proportions of isoforms B (similar to 460 kDa) and S3 (similar to 640 kDa); variations in K-d values (from 141 nM to 460 nM) as a function of the relative content in isoform S3 were observed. Altogether, these results are indicative of multiple binding by ligands that bind with different affinities to equivalent but independent sites. Thus, in plasma from heterozygous subjects, the influence of each Lp(a) isoform on fibrinolysis will depend on their affinity for fibrin and on their concentration relative to each other and to plasminogen. [References: 39]
机译：我们先前已经表明，重组载脂蛋白（a）和天然脂蛋白（a）均抑制Glu-纤溶酶原与纤维蛋白表面的结合[Fleury＆Angles-Cano（1991）Biochemistry 30，7630-7638; Rouy等。 （1992）Biochemistry 31，6332-6339]。本研究的目的是表征这种抑制作用的机制，并定义当两个不同的Lp（a）物种与纤溶酶原竞争纤维蛋白时的结合控制参数，这种情况在体内对apo杂合的受试者体内可能会发现a）特质。纤溶酶原与纤维蛋白结合的K-d为660 nM，而Lp（a）的亲和力与apo（a）大小成反比（K-d范围：50至> 500 nM）。为了确定纤溶酶原对Lp（a）结合的影响，并且相互进行了竞争实验。 Lp（a）或纤溶酶原的纤维蛋白的K-d在其他竞争者存在的情况下保持不变，而最大结合量B-max则显着降低。以类似的方式，通过使用含有不同比例的同工型B（约460 kDa）和S3（约640 kDa）的Lp（a）密度级分，证明了Lp（a）同工型之间血纤蛋白结合的竞争。观察到K-d值（从141 nM到460 nM）随同工型S3中相对含量的变化。总而言之，这些结果表明配体的多重结合，其以不同的亲和力结合到等同但独立的位点。因此，在来自杂合受试者的血浆中，每种Lp（a）同工型对血纤蛋白溶解的影响将取决于它们对血纤蛋白的亲和力以及相对于彼此和血纤维蛋白溶酶原的浓度。 [参考：39]

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号