Optical resolution of phenylthiohydantoin-amino acids by capillary electrophoresis and identification of the phenylthiohydantoin-D-amino acid residue of [D-Ala2]-methionine enkephalin.
This is an initial report to propose a protein sequence analysis system with DL differentiation using capillary electrophoresis (CE). This system consists of a protein sequencer and a CE system. After fractionation of phenyl-thiohydantoin (PTH)-amino acids using a protein sequencer, optical resolution for each PTH-amino acid is performed by CE using some chiral selectors such as digitonin, beta-escin and others. As a model peptide, [D-Ala2]-methionine enkephalin (L-Tyr-D-Ala-Gly-L-Phe-L-Met), was used and the sequence with DL differentiation was determined, with the exception of the fourth amino acid, L-Phe, using our proposed system.
Kurosu
Y
Y
JASCO Technical Research Laboratories Corporation, Tokyo, Japan.
Murayama
K
K
Shindo
N
N
Shisa
Y
Y
Ishioka
N
N
D000596:Amino Acids / Q000302:isolation & purification*; D002851:Chromatography, High Pressure Liquid; D019075:Electrophoresis, Capillary / Q000379:methods*; D004744:Enkephalin, Methionine / Q000031:analogs & derivatives* / Q000737:chemistry; D055095:Optics and Photonics; D010669:Phenylthiohydantoin / Q000737:chemistry*
D000596:Amino Acids; D010669:Phenylthiohydantoin; D004744:Enkephalin, Methionine; C013801:enkephalin-Met, Ala(2)-