Laudano A P, Doolittle R F
Science. 1981 Apr 24;212(4493):457-9. doi: 10.1126/science.7209542.
The affinity of the amino terminal tetrapeptide of the beta chain of fibrin, Gly-His-Arg-Pro, for fibrinogen dramatically increases in the presence of 2 millimolar calcium ion. In contrast, there is no significant increase in the affinity of peptides beginning with the amino terminal sequence of the fibrin alpha chain, Gly-Pro-Arg, in the presence of calcium ions, although the number of binding sites increases. In the latter case, the increased number of sites is due to the alpha chain analogs binding to the site ordinarily occupied by the beta chain analogs. These results indicate that structures at the amino terminus of the fibrin beta chain play a more important role in fibrin polymerization when calcium ions are present.
纤维蛋白β链氨基末端四肽Gly-His-Arg-Pro对纤维蛋白原的亲和力在2毫摩尔钙离子存在时显著增加。相比之下,尽管结合位点数量增加,但以纤维蛋白α链氨基末端序列Gly-Pro-Arg开头的肽在钙离子存在时亲和力没有显著增加。在后一种情况下,位点数量增加是由于α链类似物与通常由β链类似物占据的位点结合。这些结果表明,当存在钙离子时,纤维蛋白β链氨基末端的结构在纤维蛋白聚合中起更重要的作用。