PROTHYMOSIN-ALPHA - EFFICIENT SEQUENCE DETERMINATION BY EXPERIMENTAL AND THEORETICAL CAPILLARY ELECTROPHORETIC SUPPORT

A rapid and efficient primary structure elucidation of prothymosin (Pr oT alpha) and its enzymatic fragments was performed by a combination o f matrix-assisted laser desorption ionization mass spectrometry (MALDI ), automatic N-terminal Edman degradation, and the available theoretic al predictions of electrophoretic mobility in capillary electrophoresi s (CE) as a basis suggesting active sites of ProT alpha in the differe nt bioassays.