Han K, Davril M, Lohez M, Moczar M, Moczar E
Paroi Arterielle. 1979 Jul;5(2):69-74.
Kappa-Elastin is exhaustively guanidinated in order to chemically modify the pre-existing lysine content to homoarginine. However the pre-existing lysine content is only modified to homoarginine content about 50 p.cent. The other lysyl-bonds are buried or/and engaged to aldi-imine bonds or other bonds. Therefore the first guanidinated kappa-Elastin is submitted to partial acide hydrolysis (HCL, 1 N, 110 degrees C for 2 hours) and submitted to a second exhaustive guanidination. The pre-existing lysin content in kappa-Elastin almost quantitively disappeared and is transformed to the corresponding homoarginine. These results are similar to those obtained by photolysis of (Iso) desmosine residues by UV light which will liberate "new" lysine containing peptides from kappa-Elastin.
κ-弹性蛋白被彻底胍基化，以便将预先存在的赖氨酸含量化学修饰为高精氨酸。然而，预先存在的赖氨酸含量仅被修饰为约50%的高精氨酸含量。其他赖氨酰键被掩埋或/和参与醛亚胺键或其他键。因此，首先将胍基化的κ-弹性蛋白进行部分酸水解（1N盐酸，110℃，2小时），然后进行第二次彻底胍基化。κ-弹性蛋白中预先存在的赖氨酸含量几乎定量消失，并转化为相应的高精氨酸。这些结果与通过紫外线光解（异）锁链素残基从κ-弹性蛋白中释放出“新”的含赖氨酸肽所获得的结果相似。
