Document Detail


13C-NMR spectral study of reductively [13C]methylated glycophorin B.
MedLine Citation:
PMID:  6487642     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Glycophorin BN was reductively [13C]methylated and the 13C chemical shift of the N-terminal [13C]dimethyl-leucine residue was monitored as a function of pH. These results were compared to the pH-dependent chemical shift studies of the N-terminal [13C]dimethylleucine residues of intact glycophorin AN and N-terminal glyco-octapeptide AN. The results indicate that the titration data for [13C]dimethylleucine of glycophorin BN more closely resembles the titration data observed for the [13C]dimethylleucine residue of the N-terminal glyco-octapeptide AN rather than for the [13C]dimethylleucine residue of intact glycophorin AN. Integration of the 13C resonances indicated that glycophorin BN contains 3-4 lysine residues.
Authors:
R D Carter; J R Brooks; K Dill
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  790     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1984 Nov 
Date Detail:
Created Date:  1984-12-18     Completed Date:  1984-12-18     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  285-7     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Glycophorin*
Humans
Hydrogen-Ion Concentration
MNSs Blood-Group System
Magnetic Resonance Spectroscopy
Methylation
Oxidation-Reduction
Sialoglycoproteins*
Chemical
Reg. No./Substance:
0/Glycophorin; 0/MNSs Blood-Group System; 0/Sialoglycoproteins

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


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