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- W84208784 abstract "Intrinsic factor (IF) is produced in foregut tissues of mammals and mediates the uptake of cobalamin (Cbl, vitamin BI2). It is a protein with unusual properties, being soluble and functional at very acidic pH. This chapter discusses the expression of functional IF using recombinant baculovirus. The majority of recombinant IF produced in the baculovirus system is nonglycosylated. Insect cells do not often add the larger complex oligosaccharide side chains seen in glycoproteins of higher eukaryotes, but they do provide trimmed high-mannose units. Glycosylation of IF only during the first 24 hours could be due either to efficient glycosylation only when expression of recombinant protein is at a low level or to direct inhibition of host cell glycosylation as infection proceeds. The composition of the carbohydrate side chains of baculovirus-derived recombinant IF is not known, but it is probably different from that of native gastric IF. Despite this difference, the functional characteristics of the purified recombinant IF are identical to those of native IF." @default.
- W84208784 created "2016-06-24" @default.
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- W84208784 date "1997-01-01" @default.
- W84208784 modified "2023-09-29" @default.
- W84208784 title "Expression of functional intrinsic factor using recombinant baculovirus" @default.
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- W84208784 doi "https://doi.org/10.1016/s0076-6879(97)81031-2" @default.
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