Abstract
It has been detected that racemization of amino acids in metabolically stable proteins of living mammals takes place (1–4) and as a consequence the protein-structure function relationship may be altered (5). Thus in vitro and in vivo analysis of racemic amino acids is very important. Besides enantiomeric purity becomes very significant when only one of the enantiomers has a potential biological activity for example L-DOPA (3,4-dihydroxypheny 1 alanine) is an important drug for treating Parkingson's disease. The measurement of specific rotation is a common and well accepted method for evaluating hydrophile-hydrophile interactions between the second carboxyl group of amino acid and the alkaline substructures of adenine (probably hydrogen-bond formation); hydrophobe-hydrophobe interactions between the apolar sidechain of the amino acid and the corresponding adenine substructures.