摘要
从浸酸牛皮胶原和修饰胶原为作用物，采用氨基酸分析方法研究了胶原与N-（β-羟乙基）■唑烷（简称OX－2）反应过程中几种活性基的作用。结果表明，OX-2与胶原酪氨酸残基的酚环发生了不可逆结合，此结合可能是OX-2从羟甲基的形式与酪氨酸酚环发生缩合形成的；OX－2与组氨酸残基的咪唑基也发生了不可逆结合，其反应程度可能要受到胶原中微环境的影响；OX－2与ε-氨基、胍基等均未形成不可逆给合。
The reaction of N - (β- hydroxylethyl )oxazolidine (OX - 2 ) with some active groups in col lagen has been studied by amino acid analysis using pickled cattle hide collagen and modified collagen as substrates. The results have indicated that irreversible binding between OX - 2 and tyrosine residues occurs during the reactions which may be attributed to the condensation of hydroxymethyl of OX - 2 with phenolic groups, the irreversible binding also occurs be tween imidazole groups and OX-2 which seems to be affected by miniature surroundings of the groups, and no irreversible binding occurs between OX-2 and ε-amino groups as well as guanidino groups
出处
《中国皮革》
CAS
北大核心
1997年第2期10-12,共3页
China Leather
