Omichi K, Savic G, Yoshida A
Int J Biochem. 1983;15(11):1345-51. doi: 10.1016/0020-711x(83)90025-3.
The sialic acid residues of human alpha 1-protease inhibitor were modified by periodate oxidation and subsequent reductive amination with ethanolamine and sodium cyanoborohydride. The modified inhibitor retained its original trypsin inhibitory activity and was not digested by neuraminidase from Clostridium perfringens. The modified inhibitor disappeared from rat blood circulation at the same rate as the native inhibitor.
人α1-蛋白酶抑制剂的唾液酸残基通过高碘酸盐氧化，随后与乙醇胺和氰基硼氢化钠进行还原胺化反应进行修饰。修饰后的抑制剂保留了其原始的胰蛋白酶抑制活性，并且不会被产气荚膜梭菌的神经氨酸酶消化。修饰后的抑制剂在大鼠血液循环中消失的速度与天然抑制剂相同。
