Document Detail


Fish egg polysialoglycoproteins: circular dichroism and proton nuclear magnetic resonance studies of novel oligosaccharide units containing one sialidase-resistant N-glycolylneuraminic acid residue in each molecule.
MedLine Citation:
PMID:  6320865     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Long-core units having the common sequence Ga1NAc beta 1 leads to 4(NeuGc2 leads to 3)Ga1NAc beta 1 leads to 3Gal beta 1 leads to 4Ga1 beta 1 leads to 3Ga1NAc are one of the major constituents of rainbow trout egg polysialoglycoproteins. The existing ambiguity regarding the anomeric configuration of the sialidase-resistant unsubstituted sialyl group present in this novel type of oligosaccharide chains has been resolved by a circular dichroism difference spectral method. The fact that the negative band originating from the carbohydrate n leads to pi transition for this sialyl group was observed offers conclusive proof of the alpha-anomeric configuration. Next particularly interesting is the fact that the chemical shifts of the sialidase-resistant sialyl H-3eq and H-3ax protons were respectively found at relatively higher and lower magnetic field than for the corresponding protons of other sialyl groups. A consideration of molecular models shows that the observed anomalies are all in the directions compatible with expectations on the basis of the magnetic anisotropy effect due to the carboxylate group and steric compression effects by van der Walls interactions between groups that are sterically compressed. In addition to the observed resistance to bacterial sialidases of this sialyl group, it did not behave even as a competitive inhibitor of the sialidase, Arthrobacter ureafaciens, indicating that inaccessibility of this unique sialyl group toward the enzyme. Finally, the analysis of the proton nuclear magnetic resonances of sialidase-sensitive mono- and oligosialyl groups present in the long-core units was based on comparisons of diagnostically important regions in the spectra of homologous oligosaccharides of N-glycolylneuraminic acid.
Authors:
K Kitajima; H Nomoto; Y Inoue; M Iwasaki; S Inoue
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biochemistry     Volume:  23     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  1984 Jan 
Date Detail:
Created Date:  1984-04-11     Completed Date:  1984-04-11     Revised Date:  2003-11-14    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  310-6     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Animals
Arthrobacter / enzymology
Carbohydrate Conformation
Carbohydrate Sequence
Circular Dichroism
Clostridium perfringens / enzymology
Female
Magnetic Resonance Spectroscopy
Models, Molecular
Neuraminidase / metabolism
Oligosaccharides / isolation & purification*
Ovum / analysis*
Sialoglycoproteins / analysis*
Streptococcus / enzymology
Trout
Chemical
Reg. No./Substance:
0/Oligosaccharides; 0/Sialoglycoproteins; EC 3.2.1.18/Neuraminidase

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


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