Identification of the modifying sites of mono-PEGylated salmon calcitonins by capillary electrophoresis and MALDI-TOF mass spectrometry

J Chromatogr B Biomed Sci Appl. 2001 Apr 15;754(1):259-63. doi: 10.1016/s0378-4347(00)00599-5.

Abstract

A capillary electrophoretic method (CE) was developed for the determination of the PEG-modification sites of three positional isomers of mono-PEG modified salmon calcitonins (mono-PEG-sCTs). Resistance to proteolytic degradation on the PEG modification sites resulted in different patterns of CE electropherograms for the tryptic digested mono-PEG-sCTs isomers, and the PEG modification sites were assigned accordingly. The PEG-modification sites were also confirmed directly by determining the molecular masses of the tryptic digested PEG-modified fragments of respective mono-PEG-sCT by the matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Calcitonin / chemistry*
  • Electrophoresis, Capillary / methods
  • Isomerism
  • Molecular Sequence Data
  • Polyethylene Glycols / chemistry
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Trypsin

Substances

  • Polyethylene Glycols
  • salmon calcitonin
  • Calcitonin
  • Trypsin