Prothymosin alpha: efficient sequence determination by experimental and theoretical capillary electrophoretic support.
A rapid and efficient primary structure elucidation of prothymosin (ProT alpha) and its enzymatic fragments was performed by a combination of matrix-assisted laser desorption ionization mass spectrometry (MALDI), automatic N-terminal Edman degradation, and the available theoretical predictions of electrophoretic mobility in capillary electrophoresis (CE) as a basis suggesting active sites of ProT alpha in the different bioassays.
Weiler
A
A
Abteilung für Physikalische Biochemie, Physiologisch-chemisches Institut der Universität Tübingen, Germany.
Stoeva
S
S
Tsitsilonis
O E
OE
Voelter
W
W
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D019075:Electrophoresis, Capillary / Q000379:methods*; D008969:Molecular Sequence Data; D011498:Protein Precursors / Q000737:chemistry*; D017421:Sequence Analysis / Q000379:methods*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013947:Thymosin / Q000031:analogs & derivatives* / Q000737:chemistry
D011498:Protein Precursors; C040782:prothymosin alpha; D013947:Thymosin