Protein fragment domains identified using 2D gel electrophoresis/MALDI-TOF.
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.
Person
Maria D
MD
Division of Pharmacology and Toxicology, College of Pharmacy, The University of Texas at Austin, Austin, Texas, USA.
Shen
Jianjun
J
Traner
Angelina
A
Hensley
Sean C
SC
Lo
Herng-Hsiang
HH
Abbruzzese
James L
JL
Li
Donghui
D
D000595:Amino Acid Sequence; D015180:Electrophoresis, Gel, Two-Dimensional / Q000379:methods*; D000091342:Endoplasmic Reticulum Chaperone BiP; D006360:Heat-Shock Proteins / Q000737:chemistry; D006801:Humans; D007526:Isoelectric Point; D018832:Molecular Chaperones / Q000737:chemistry; D008969:Molecular Sequence Data; D010179:Pancreas / Q000378:metabolism; D010447:Peptide Hydrolases / Q000737:chemistry; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D040901:Proteomics / Q000379:methods*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*
D000091342:Endoplasmic Reticulum Chaperone BiP; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D010455:Peptides; D011506:Proteins; D010447:Peptide Hydrolases