Cannon D J, Davison P F
Connect Tissue Res. 1976;4(3):187-91. doi: 10.3109/03008207609152218.
The reduction of collagen with sodium [3H] borohydride in the presence of Tris buffer results in the stabilization of a Schiff base adduct which is formed between allysine residues and tris(hydroxymethyl)aminomethane. The reduced, radioactive derivative of this adduct has been identified in hydrolyzates or reduced collagen. It elutes before hydroxylysine on an amino acid analyzer column close to the position of dihydroxylysinonorleucine. Similar artifacts may occur when aldehydes present in or added to proteins react with Tris or other amines prior to reduction.
在Tris缓冲液存在的情况下，用[³H]硼氢化钠还原胶原蛋白会导致席夫碱加合物的稳定，该加合物在烯赖氨酸残基与三（羟甲基）氨基甲烷之间形成。这种加合物的还原放射性衍生物已在水解产物或还原胶原蛋白中得到鉴定。在氨基酸分析仪柱上，它在羟赖氨酸之前洗脱，靠近二羟基赖氨酰正亮氨酸的位置。当蛋白质中存在的或添加到蛋白质中的醛在还原之前与Tris或其他胺反应时，可能会出现类似的假象。
