N—(β-羟乙基)恶唑烷在胶原分子上的主要结合点的研究

The Main Binding Sites of N (β-hydroxylethyl) Oxazolidine in Collagen

以浸酸牛皮胶原为作用物,采用分子修饰方法研究了N—(β-羟乙基)恶唑烷(简称OX—2)与胶原分子中几种主要活性基的反应.胶原分子的修饰程度和OX—2结合量采用氨基酸分析、红外光谱和凯氏定氮方法测定.结果表明,在胶原分子中,氨基是OX—2的主要共价交联点,与OX—2的结合对胶原收缩温度的提高起着决定作用;羧基与OX—2不形成共价键,而以弱的离子健结合,这种结合对胶原收缩温度的提高几乎没有贡献;胍基和醇羟基在pH5～8的条件下对OX—2几乎没有交联反应活性.

The reactions of N(B-Hydroxylethyl)oxazolidine(OX - 2) and collagen have been studied by collagen molecule modification using pickled ox-hide collagen as substrates. The extent of collagen modificantion and the fixation of OX - 2 have been inspected by amino acid analysis , IR-spectra and Kjeldahl method. It has been shown that amino groups in collagen are main covalent crosslink sites of OX -2 which play a dependent role in Ts increase, carboxyl groups don't form covalent bonding but weak ionic bonding with OX -2 which scarcely contribute to the Ts increase. guanidino groups and alcoholic hydroxyl groups scarcely possess crosslinking reactivity to OX -2 over pH 5 to 8.