Document 0496
 DOCN  M9650496
 TI    Differences in the glycosylation of recombinant and native human milk
       bile salt-stimulated lipase revealed by peptide mapping.
 DT    9605
 AU    Stromqvist M; Lindgren K; Hansson L; Juneblad K; ASTRA HASSLE AB, Umea,
       Sweden.
 SO    J Chromatogr A. 1995 Dec 1;718(1):53-8. Unique Identifier : AIDSLINE
       MED/96129766
 AB    The milk of some mammals contains a bile salt-stimulated lipase (BSSL).
       Human milk BSSL is heavily glycosylated (30-40% carbohydrate) and
       present at a concentration of approximately 100-200 mg/l, thereby being
       one of the most abundant human whey proteins. BSSL has been shown to
       have an important role in the uptake of energy from human milk. The risk
       of HIV contamination has restricted the use of banked human milk for
       nutritional purposes. This has evoked an interest in the production of a
       recombinant form of the protein for supplementation of formula. We have
       produced BSSL in mouse C127 and hamster CHO cells, and used
       chromatographic methods for the characterization of the products. This
       study was focused on study of the glycosylation of the protein by using
       peptide mapping and isolation of glycosylated fragments. The results
       show how human BSSLs from different sources differ both in extent of
       glycosylation, in glycan heterogeneity, and in lectin binding.
 DE    Animal  Cells, Cultured  Chromatography, Gel  Cyanogen Bromide
       Glycoproteins/*CHEMISTRY  Glycosylation  Hamsters  Human
       Lectins/METABOLISM  Lipase/*CHEMISTRY  Mice  Milk/*ENZYMOLOGY  Molecular
       Weight  Peptide Fragments/ANALYSIS/CHEMISTRY  Peptide Mapping/METHODS
       Peptide Peptidohydrolases/METABOLISM  Recombinant Proteins/CHEMISTRY
       Support, Non-U.S. Gov't  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).