Differences in the glycosylation of recombinant and native human milk bile salt-stimulated lipase revealed by peptide mapping
| Autor: | Kristina Juneblad, Lennart Hansson, Kerstin Lindgren, Mats Strömqvist |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Glycan
Glycosylation Peptide Mapping Biochemistry Analytical Chemistry law.invention Mice chemistry.chemical_compound law Cricetinae Lectins Endopeptidases Sterol esterase Animals Humans Cyanogen Bromide Lipase Cells Cultured Glycoproteins chemistry.chemical_classification biology Chemistry Chinese hamster ovary cell Organic Chemistry General Medicine Sterol Esterase Peptide Fragments Recombinant Proteins Molecular Weight Milk Chromatography Gel biology.protein Recombinant DNA Cyanogen bromide Glycoprotein |
| Zdroj: | Journal of Chromatography A. 718:53-58 |
| ISSN: | 0021-9673 |
| DOI: | 10.1016/0021-9673(95)00632-x |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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