Sato H, Swadesh J K
Department of Polymer Chemistry, Kyoto University, Japan.
Int J Biol Macromol. 1993 Dec;15(6):323-7. doi: 10.1016/0141-8130(93)90048-q.
Fragment X (LMrFX) was obtained as low molecular weight preparations from a late stage 2 plasmin digest of human fibrinogen. The thrombin-treated LMrFX preparations, which resulted in impaired polymerization, were further subfractionated into polymerized and non-polymerized components. The fractions were examined by SDS-PAGE and immunochemical methods. In polymerized fractions, more peptide bands were observed on SDS-PAGE in the reduced state than in non-polymerized fractions. Both fractions contained a similar number of internal cleavages in the A alpha, B beta and gamma chains, which are linked by disulfide bonds. Thus, the partial deficiencies in polymerization sites of the carboxy terminal region of the gamma chain and the amino terminal portions of the B beta chain, as well as internal cleavage, were considered to participate in the impairment of the thrombin-induced polymerization of LMrFX.
片段X（LMrFX）是从人纤维蛋白原的2期晚期纤溶酶消化产物中获得的低分子量制剂。经凝血酶处理的LMrFX制剂导致聚合受损，进一步亚分级为聚合和未聚合成分。通过SDS-PAGE和免疫化学方法检查这些级分。在聚合级分中，与未聚合级分相比，在还原状态下的SDS-PAGE上观察到更多的肽带。两个级分在通过二硫键连接的Aα、Bβ和γ链中含有相似数量的内部切割。因此，γ链羧基末端区域和Bβ链氨基末端部分的聚合位点部分缺陷以及内部切割被认为参与了凝血酶诱导的LMrFX聚合受损。
