A stabilised tris(hydroxymethyl)aminomethane adduct in reduced collagen.
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.
D000498:Allyl Compounds; D000818:Animals; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D003094:Collagen; D006868:Hydrolysis; D008239:Lysine; D010084:Oxidation-Reduction; D051381:Rats; D014325:Tromethamine
D000498:Allyl Compounds; D014325:Tromethamine; D003094:Collagen; D008239:Lysine