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Updated: Aug 6, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
Intestinal glycosyl-transferase activities. Nutritional regulation by a chemically-modified protein: methionyl-casein
M C Biol1, A Martin, H Gaertner
1Department of General and Medical Biochemistry, Lyon-Sud Medical School, INSERM-CNRS U 189, University of Lyon, France.
Abstract:
In order to estimate the effect of a chemically modified casein, glycosylation processes were studied in rats fed a diet containing this protein. Two groups of rats were fed either a methionyl-casein diet or a normal casein diet. The methionyl-casein was enriched in methionine by covalent linkage of this amino-acid. The nutritional data (growth, protein intake...) were not modified by the diet. The microsomal N-acetylgalactosaminyl- and fucosyl-transferase activities were unaffected by the diet. On the contrary, the soluble fucosyl-transferase activity was enhanced and the activation of fucose transfer in cytosol from methionyl-casein-diet fed rats disappeared after enzyme purification by DEAE-cellulose chromatography. The activation was not explained by changes in some interfering reactions (glycosyl-nucleotide pyrophosphatase, oxidase, protease activities).
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