[Neuraminidase activity of the L forms of Erysipelothrix rhusiopathiae].
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Biomedical subjects
Publications and source records attributed to I Abrashev.
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A number of reducing agents used for removing the excess of periodate in the reaction of the neuraminidase (EC 3.2.1.18) activity measuring by the thiobarbituric acid technique were compared. The toxic reagent sodium arsenite may be replaced by a 20% solution of ascorbic acid. The modified technique of the neuraminidase activity determining can be used in case of both high-molecular weight substrate ovomucin and low-molecular weight substrate-glycomacropeptide from milk whey.
Glycomacropeptide from milk was studied; its molecular mass and amino acid composition were evaluated. When the glycomacropeptide was used as a substrate of neuraminidase, it exhibited many advantages as compared with ovomucin (high molecular substrate of the enzyme) due to increased content of sialic acids in the glycomacropeptide composition and to high solubility.