A method for the determination of free neuraminic acid split from red blood cell receptors by attached Newcastle disease virus during simultaneous elution and hemolysis

1980 ◽  
Vol 36 (3) ◽  
pp. 370-371 ◽  
Author(s):  
B. Rivetz ◽  
M. A. Lipkind ◽  
Esther Shichmanter ◽  
E. Bogin
Keyword(s):  
Blood Cell ◽  
Newcastle Disease Virus ◽  
Disease Virus ◽  
Red Blood Cell ◽  
Newcastle Disease ◽  
Neuraminic Acid ◽  
Cell Receptors

Kinetische und chemische Untersuchungen über den Abbau von Di-N-acetylneuraminosyl-lacto-N-tetraose durch Neuraminidasen von Myxoviren und Vibrio cholerae / Kinetic and Chemical Experiments about the Decay of Di-N-acetylneuraminosyl-lacto-N-tetraose by Neuraminidases of Myxoviruses and Vibrio cholerae

1971 ◽  
Vol 26 (10) ◽  
pp. 1049-1051 ◽  
Author(s):  
Hubertus Von Nicolai ◽  
Rudolf Drzeniek ◽  
Fritz Zilliken
Keyword(s):  
Human Milk ◽  
Newcastle Disease Virus ◽  
Vibrio Cholerae ◽  
Disease Virus ◽  
Newcastle Disease ◽  
Hydrolytic Activity ◽  
Neuraminic Acid ◽  
Structural Determination ◽  
Experimental Conditions

The splitting capacity of different neuraminidases (sialidases) has been tested on di-N-acetyl-neuraminosyl-lacto-N-tetraose from human milk. The substrate contains two residues of N-acetyl-neuraminic acid (NeuNAc), linked in (a, 2 → 3) position to D-galactose at the non-reducing end and in (a, 2 → 6) position to the adjacent N-acetyl-D-glucosamin. Vibrio cholerae neuraminidase releases both NeuNAc molecules. Newcastle disease virus neuraminidase as well as the enzyme from fowl plague virus cleave the (a, 2→3) linkage preferentially. The hydrolytic activity of both virus enzymes towards the (a, 2 → 6) linkage is highly reduced. Under specified experimental conditions the enzymes are useful for the structural determination of NeuNAc linkages in oligosaccharides.

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