Le Glédic S, Périn J P, Bonnet F, Jollès P
J Biol Chem. 1983 Dec 25;258(24):14759-61.
The cyanogen bromide (CNBr) fragments of the two link proteins (LP) were examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The observed apparent molecular weight difference between LP1 (Mr = 44,500) and LP2 (Mr = 48,500) was the reflect of a molecular weight difference between their NH2-terminal CNBr fragments (Mr = 19,000 and 24,000 for LP1 and LP2, respectively). The latter are glycosylated contrary to the COOH-terminal parts of the molecules. Fluorhydric acid/pyridine treatment suggests that LP1 and LP2 have a protein core of identical size. They differ from their common tryptic fragment (T-G200-3 fraction) by the presence of an additional short peptide. The latter was highly glycosylated in LP2 but not in LP1. Deglycosylation together with CNBr treatment corroborates the hypothesis that LP1 and LP2 possess a similar protein core.
通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳对两种连接蛋白（LP）的溴化氰（CNBr）片段进行了检测。观察到LP1（Mr = 44,500）和LP2（Mr = 48,500）之间明显的分子量差异反映了它们NH2末端CNBr片段之间的分子量差异（LP1和LP2的Mr分别为19,000和24,000）。与分子的COOH末端部分相反，后者是糖基化的。氢氟酸/吡啶处理表明LP1和LP2具有相同大小的蛋白质核心。它们与共同的胰蛋白酶片段（T-G200-3组分）的不同之处在于存在一个额外的短肽。后者在LP2中高度糖基化，但在LP1中未糖基化。去糖基化与CNBr处理一起证实了LP1和LP2具有相似蛋白质核心的假设。
