Document Detail


C-terminal sequencing of protein. A novel partial acid hydrolysis and analysis by mass spectrometry.
MedLine Citation:
PMID:  1606956     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Peptides or proteins were hydrolyzed by vapors of 90% pentafluoropropionic acid or heptafluorobutyric acid at 90 degrees C for various time periods. The hydrolyzate mixtures analyzed by both fast-atom-bombardment and electrospray ionization mass spectrometry showed a series of C-terminal successive degradation molecular ions. The degradation reaction may be due to the selective formation of an oxazolone ring at the C-terminal amino acid, followed by hydrolytic removal of the C-terminal amino acid. The major side reactions were cleavages of the peptide bonds at the C side of the internal aspartic acid residue and the N side of serine residue.
Authors:
A Tsugita; K Takamoto; M Kamo; H Iwadate
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  206     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  1992 Jun 
Date Detail:
Created Date:  1992-07-23     Completed Date:  1992-07-23     Revised Date:  2007-07-23    
Medline Journal Info:
Nlm Unique ID:  0107600     Medline TA:  Eur J Biochem     Country:  GERMANY    
Other Details:
Languages:  eng     Pagination:  691-6     Citation Subset:  IM    
Affiliation:
Research Institute for Biosciences, Science University of Tokyo, Yamazaki, Japan.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Fluorocarbons
Glucagon / chemistry
Hydrolysis
Mass Spectrometry*
Molecular Sequence Data
Peptide Fragments / chemistry*
Spectrometry, Mass, Fast Atom Bombardment
Chemical
Reg. No./Substance:
0/Fluorocarbons; 0/Peptide Fragments; 375-22-4/perfluorobutyric acid; 422-64-0/perfluoropropionic acid; 9007-92-5/Glucagon

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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