King T P, Zhao S W, Lam T
Biochemistry. 1986 Sep 23;25(19):5774-9. doi: 10.1021/bi00367a064.
Proteins can be modified at their amino groups under gentle conditions to contain an average of three to six aryl aldehyde or acyl hydrazide groups. These two types of modified proteins at about 10 microM concentration condense with each other at pH approximately 5 to form conjugates linked by hydrazone bonds. Under proper conditions conjugates mainly of dimers and trimers in size or, if desired, higher oligomers can be obtained. The conjugates can be dissociated to their individual protein components by an exchange reaction with an excess of acetyl hydrazide. The reversible hydrazone bonds of conjugates can be reduced with NaCNBH3 to give stable hydrazide bonds. The stability of protein-hydrazone conjugates was found to be significantly greater than that of the model compound, the N-acetylhydrazone of p-carboxybenzaldehyde. This difference is believed to result from the presence of multiple hydrazone linkages in protein conjugates.
在温和条件下，蛋白质的氨基可被修饰，使其平均含有三到六个芳基醛或酰肼基团。这两种浓度约为10微摩尔的修饰蛋白质在pH值约为5时相互缩合，形成通过腙键连接的共轭物。在适当条件下，可获得主要为二聚体和三聚体大小的共轭物，或者如果需要，也可获得更高的寡聚体。通过与过量的乙酰肼进行交换反应，共轭物可解离为其各自的蛋白质组分。共轭物的可逆腙键可用NaCNBH3还原，得到稳定的酰肼键。发现蛋白质 - 腙共轭物的稳定性明显高于模型化合物对羧基苯甲醛的N - 乙酰腙。据信这种差异是由于蛋白质共轭物中存在多个腙键。
