Abstract
L-Aspartate and L-serine were found to undergo amino acid racemization in brain myelin basic protein (MBP) of aging humans. The observed racemization was different in each chromatographically purified MBP isoform. Pepsin digestion of MBP produced three peptides, each of which exhibited different degrees of racemization of the same amino acids. MBP isolated by the same method from rat and guinea pig brain showed little accumulation of D-amino acids. Total MBP isolated from SDS-polyacrylamide disc gel electrophoresis of total human myelin proteins (delipidated myelin) was racemized to the same extent as purified MBP, indicating that the racemization observed was not an artifact of the isolation procedure. Myelin proteolipid protein from the same gel was racemized approximately half as much as MBP. The age and environment of the aspartates and serines in myelin proteins may strongly affect their observed racemizations.
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