McKillop_2004_Acta.Paediatr_93_10

Bile salt-stimulated lipase (BSSL) in human milk exists in multiple molecular forms and it has been shown that approximately one-third of lactating mothers secrete two forms. AIM: to determine the structural features of BSSL that may give rise to this heterogeneity.
METHODS: Oligosaccharides present in the proline-rich region in the C-terminus of BSSL were investigated using deglycosylating enzymes and lectin affinity probing to determine the origin of the multiple molecular forms.
RESULTS: It was found that the variability in the molecular mass of BSSL is due predominantly to glycosylation. The molecular forms contain similar sugar chains; all forms possess the core disaccharide Galbeta1-3GalNAc and beta-D-galactose, fucose linked at alpha1-6 and sialic acid linkage alpha2-3 to galactose. CONCLUSION: The molecular mass difference in the BSSL molecular forms cannot be attributed to the type of carbohydrate moiety in the sugar chains of the N- and O-linked sites suggesting that the differences arise from the extent or quantity of glycosylation. The oligosaccharides in the C-terminal region contain Lewis x and b and, less prominently, Lewis a antigenic structures. Owing to the presence of these blood-group-related antigenic determinants, the C-terminal region of BSSL may have an adhesive function in cell-cell interactions.