Gruen L C, King N L, Kurth L, McKenzie L J
Int J Pept Protein Res. 1982 Nov;20(5):401-7. doi: 10.1111/j.1399-3011.1982.tb03059.x.
Enzymic hydrolysis, followed by amino acid analysis, provided no evidence for the presence of epsilon-(gamma-glutamyl) lysine or other isopeptide crosslinks in connectin. Gel elecrrophoresis in the presence of sodium dodecyl sulphate did not reveal any difference in connectin between normal and lathyritic muscle, indicating that lysyl oxidase does not initiate cross-link formation in connectin. Although connectin may be covalently crosslinked by some unknown mechanism, the available evidence suggests that the subunit of MW approximately to 900 000 is synthesised as a single polypeptide chain. In developing fetal muscle, myosin heavy chains are apparent some weeks earlier than connectin. This, together with the known susceptibility of connectin to hydrolysis, suggests that connectin exists in an exposed environment rather than as a core to the thick filament.
酶解后进行氨基酸分析，结果未发现连接蛋白中存在ε-（γ-谷氨酰基）赖氨酸或其他异肽交联键。在十二烷基硫酸钠存在的情况下进行凝胶电泳，未发现正常肌肉和患骨生成障碍病的肌肉之间的连接蛋白有任何差异，这表明赖氨酰氧化酶不会引发连接蛋白中的交联形成。尽管连接蛋白可能通过某种未知机制发生共价交联，但现有证据表明，分子量约为900000的亚基是作为一条单一的多肽链合成的。在发育中的胎儿肌肉中，肌球蛋白重链比连接蛋白早几周出现。这一点，再加上已知连接蛋白易被水解，表明连接蛋白存在于一个暴露的环境中，而不是作为粗肌丝的核心。
