Document Detail


Non-enzymic glycation of proteins: analysis of N-(1-deoxyhexitol-1-yl)amino acids by high-performance liquid chromatography.
MedLine Citation:
PMID:  3779697     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A method for determining the extent of non-enzymic glycation (originally called "glycosylation") of both lysyl and N-terminal residues of a protein is described. The glycated protein is treated with sodium borohydride, and is then subjected to acid-catalysed hydrolysis. The resulting N-(1-deoxy-D-hexitol-1-yl)amino acids are separated by cation-exchange high-performance liquid chromatography (l.c.), and detected by a post-column reaction with periodate. The method has been applied successfully to samples of human hemoglobin and human serum albumin, for measurement of numbers of valine-attached and of lysine-attached N-(1-deoxy-D-fructos-1-yl) groups per protein molecule.
Authors:
D J Walton; J D McPherson
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Carbohydrate research     Volume:  153     ISSN:  0008-6215     ISO Abbreviation:  Carbohydr. Res.     Publication Date:  1986 Oct 
Date Detail:
Created Date:  1987-01-02     Completed Date:  1987-01-02     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0043535     Medline TA:  Carbohydr Res     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  285-93     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Amino Acids
Borohydrides
Carbohydrates
Chromatography, High Pressure Liquid / methods
Glycoproteins / chemical synthesis*
Hemoglobins
Humans
Hydrolysis
Serum Albumin
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Borohydrides; 0/Carbohydrates; 0/Glycoproteins; 0/Hemoglobins; 0/Serum Albumin

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


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