“…33 . 34 ) Soon after the completion of our experiment, a work on the separation of tri-and tetrasaccharides from K-casein and on the determination of their chemical structures 6]-GalNAc) by alkali treatment and GLCmasspectrometry analysis was reported by Fournet et al 8 ) The structure of the trisaccharide proposed coincides well with ours. In their study, however, the partial structure between D-Gal and GalNAc was determined from gaschromatographic data on D-Gal and GalNAcItol, and the molar ratio was measured to be 1 : 0.45.…”
“…33 . 34 ) Soon after the completion of our experiment, a work on the separation of tri-and tetrasaccharides from K-casein and on the determination of their chemical structures 6]-GalNAc) by alkali treatment and GLCmasspectrometry analysis was reported by Fournet et al 8 ) The structure of the trisaccharide proposed coincides well with ours. In their study, however, the partial structure between D-Gal and GalNAc was determined from gaschromatographic data on D-Gal and GalNAcItol, and the molar ratio was measured to be 1 : 0.45.…”
“…Such an observation has already been made by numerous authors: Sinkinson and Wheelock, 1970;Doi et al, 1979;Fournet et al, 1979;Jollès and Fiat, 1979;Addeo et al, 1984;Van Hooydonk et al, 1984. It has been attributed to a reduced accessibility to chymosin of the glycosylated sites of x-casein which would have higher electronegativity than the carbohydrate-free forms (Van Hooydonk et al, 1984).…”
Section: Phe1os-met106 Linkage In Glycosylatedmentioning
Summary -The kinetics of release of the glycosylated and carbohydrate-free forms of caseinomacropeptide (CMP) was studied in renneted rawand UHT (140 oC for 10 s) milks. The new chromatographic method utilized allowed quantitative determinations of both molecular torrns. UHT treatment leads to a 40% decrease of the final content in glycosylated forms compared to the value determined in raw milk. The results obtained show that carbohydrate-free ic-casein constitutes 52% of whole x-cassin. When milk is UHT treated,~-Iactoglobulin only seems to influence the release of the glycosylated form. Nevertheless, no conclusion can be drawn concerning the localization in the micellar structure of both molecular forms of x-caseln.
“…K-Casein has mucin-type carbohydrate chains with the structures NANA-Gal-GaINAc-Thr, GalGaINAc(NANA)-Thr, and NANA-GalGaINAc(NANA)-Thr. 2,3) The observed microheterogeneity of Kcasein has been attributed to variations in the amount of carbohydrate chains. 4 ) We fractionated K-casein A into 9 subcomponents containing 0 to 8 sialic acids and 0 to 4 GaINAc, and found that the carbohydrate mOIetIes strongly enhance the micellestabilizing ability of K-casein.5) The carbohydrate chains of K-casein are synthesized by the successive action of three glycosyl transferases; UDP-N-acetylgalactosamine: K-casein polypeptide N-acetylgalactosaminyltransferase (Nacetylgalactosaminyltransferase ),.…”
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