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Hoppe Seylers Z Physiol Chem. 1976 Apr;357(4):559-66.

Demonstration of neuraminidase activity in human blood serum and human milk using a modified, radioactively labelled alpha1-glycoprotein as substrate.


N-Acetylneuramini acid of alpha1-glycoprotein was oxidized with a small molar excess of periodate and reduced with tritium-labelled borohydride. By this method about 50% of the N-acetylneuraminic acid was converted to its radioactively labelled C8-analog and 25% to its C7-analog. Using this modified alpha1-glycoprotein as substrate, minimum neuraminidase concentrations of 10(-18) units/ml, related to the activity of neuraminidase from Vibrio cholerae, could be determined. Neuraminidase activity was demonstrated in 95% of the sera or blood plasma samples from a series of 417 healthy or ill human individuals and in milk samples from 5 different donors. The neuraminidase in both serum and milk had optimal activity at pH 5.5. On an average, 10(-10) neuraminidase units were found in 1 ml serum and 10(-8) units in 1 ml milk. Although the neuraminidase activities in the sera varied, a correlation with definite pathological states is not yet possible. N-Acetylneuraminate pyruvate-lyase activity could not be detected in human serum.

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