Protein fragment domains identified using 2D gel electrophoresis/MALDI-TOF

J Biomol Tech. 2006 Apr;17(2):145-56.

Abstract

We previously reported a protein expression profiling experiment conducted on human pancreatic tissues using 2D gel electrophoresis and mass spectrometry. Here, 18 spots that were identified in the gel at molecular weights more than 10 kDa lower than database values are characterized. The matrix-assisted laser desorption/ionization mass spectrometry coverage is sufficient to identify the protein region present in each spot. Most of the fragments correspond to processed chains and known structural or functional domains, which may result from limited proteolysis.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Electrophoresis, Gel, Two-Dimensional / methods*
  • Endoplasmic Reticulum Chaperone BiP
  • Heat-Shock Proteins / chemistry
  • Humans
  • Isoelectric Point
  • Molecular Chaperones / chemistry
  • Molecular Sequence Data
  • Pancreas / metabolism
  • Peptide Hydrolases / chemistry
  • Peptides / chemistry
  • Protein Conformation
  • Protein Structure, Tertiary
  • Proteins / chemistry*
  • Proteomics / methods*
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / methods*

Substances

  • Endoplasmic Reticulum Chaperone BiP
  • Heat-Shock Proteins
  • Molecular Chaperones
  • Peptides
  • Proteins
  • Peptide Hydrolases