TY - JOUR
T1 - Variation in the Glycosylation Pattern of Bovine K-Casein with Micelle Size and Its Relationship to a Micelle Model
AU - Slattery, Charles W.
N1 - 44 (51) , 17027-17036.https://doi.org/10.1021/bi051352r
PY - 1978
Y1 - 1978
N2 - Bovine casein micelles were separated into seven size classes and the supernatant by differential centrifugation. The K-casein was isolated from each class, and s020.w, the weight-average molecular weight (Mw), the hexose content, and the proportion glycosylated were determined for each. Glycosylation appears to follow complete micelle formation so that surface or near-surface K-casein is modified while that incorporated into the interior is unchanged. The largest micelles seem to have little interior K-casein but instead act as a coat-core system with K-casein all on the surface. The single class of largest micelles, fraction 1, contained K-casein with the highest Mw, the largest amount of associated hexose and a proportion glycosylated approaching that of supernatant K-casein. The proportion of glycosylated K-casein in the remaining micelle size classes appeared to be inversely related to micelle size with the exception of fraction 2 which probably contained some fraction 1-type micelles. The hexose to glycosylated protein ratio generally followed the MW and s020,W values. Further fractionation of the K-caseins according to polymer size by gel filtration revealed that, except for the K-casein from the largest micelles, hexose content and the hexose to glycosylated protein ratio were greatest for the larger sized polymers and decreased slightly as polymer size decreased. A higher hexose content for K-casein polymers of high molecular weight than for those of lower molecular weight would favor a previously proposed model [Slattery, C. W., & Evard, R. (1973) Biochim. Biophys. Acta 317. 529].
AB - Bovine casein micelles were separated into seven size classes and the supernatant by differential centrifugation. The K-casein was isolated from each class, and s020.w, the weight-average molecular weight (Mw), the hexose content, and the proportion glycosylated were determined for each. Glycosylation appears to follow complete micelle formation so that surface or near-surface K-casein is modified while that incorporated into the interior is unchanged. The largest micelles seem to have little interior K-casein but instead act as a coat-core system with K-casein all on the surface. The single class of largest micelles, fraction 1, contained K-casein with the highest Mw, the largest amount of associated hexose and a proportion glycosylated approaching that of supernatant K-casein. The proportion of glycosylated K-casein in the remaining micelle size classes appeared to be inversely related to micelle size with the exception of fraction 2 which probably contained some fraction 1-type micelles. The hexose to glycosylated protein ratio generally followed the MW and s020,W values. Further fractionation of the K-caseins according to polymer size by gel filtration revealed that, except for the K-casein from the largest micelles, hexose content and the hexose to glycosylated protein ratio were greatest for the larger sized polymers and decreased slightly as polymer size decreased. A higher hexose content for K-casein polymers of high molecular weight than for those of lower molecular weight would favor a previously proposed model [Slattery, C. W., & Evard, R. (1973) Biochim. Biophys. Acta 317. 529].
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U2 - 10.1021/bi00599a025
DO - 10.1021/bi00599a025
M3 - Article
C2 - 629950
SN - 0006-2960
VL - 17
SP - 1100
EP - 1104
JO - Biochemistry
JF - Biochemistry
IS - 6
ER -