| C-terminal sequencing of protein. A novel partial acid hydrolysis and analysis by mass spectrometry. | |
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MedLine Citation:
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PMID: 1606956 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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A Tsugita; K Takamoto; M Kamo; H Iwadate |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: European journal of biochemistry / FEBS Volume: 206 ISSN: 0014-2956 ISO Abbreviation: Eur. J. Biochem. Publication Date: 1992 Jun |
Date Detail:
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Created Date: 1992-07-23 Completed Date: 1992-07-23 Revised Date: 2007-07-23 |
Medline Journal Info:
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Nlm Unique ID: 0107600 Medline TA: Eur J Biochem Country: GERMANY |
Other Details:
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Languages: eng Pagination: 691-6 Citation Subset: IM |
Affiliation:
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Research Institute for Biosciences, Science University of Tokyo, Yamazaki, Japan. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Fluorocarbons Glucagon / chemistry Hydrolysis Mass Spectrometry* Molecular Sequence Data Peptide Fragments / chemistry* Spectrometry, Mass, Fast Atom Bombardment |
| Chemical | |
Reg. No./Substance:
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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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