N-glycosylation of a baculovirus-expressed recombinant glycoprotein in three insect cell lines

In Vitro Cellular and Developmental Biology - Animal

Volumn 34, Issue 2, 1998, Pages 101-108

  Kulakosky, P C ^a  

^a Cornell University   (United States)

Author keywords

Alkaline phosphatase; Baculovirus; Glycoprotein; Insect cell culture; Spodopterafrugiperda; Trichoplusia ni

Indexed keywords

ALKALINE PHOSPHATASE; GLYCOPROTEIN; MANNOSE; OLIGOSACCHARIDE; PHOSPHATE; RECOMBINANT GLYCOPROTEIN; UNCLASSIFIED DRUG;

AFFINITY CHROMATOGRAPHY; ANIMAL CELL; ARTICLE; BACULOVIRUS; CELL MIGRATION; CONTROLLED STUDY; INSECT; LEPIDOPTERA; NONHUMAN; PROTEIN EXPRESSION; PROTEIN GLYCOSYLATION; PROTEIN PURIFICATION; VIRUS EXPRESSION;

ANIMALIA; ARACHNIDA; HEXAPODA; INSECTA; LEPIDOPTERA; SPODOPTERA FIUGIPERDA; SPODOPTERA FRUGIPERDA; TRICHOPLUSIA NI; UNIDENTIFIED BACULOVIRUS;

EID: 0032427728     PISSN: 10712690     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11626-998-0091-0     Document Type: Article

References (5)

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2. Altmann, F.; Schwihla, H.; Staudacher, E., et al. Insect cells contain an unusual, membrane-bound β-N-acetylglucosaminidase probably involved in the processing of protein N-glycans. J. Biol. Chem. 29:17341-17349; 1995.
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5. Davidson, D. J.; Castellino, F. J. Asparagine-linked oligosaccharide processing in lepidopteran insect cells; temporal dependence of the nature of the oligosaccharides assembled on asparagine-289 of recombinant human plasminogen produced in baculovirus vector infected Spodoptera frugiperda (IPLB-SF-21AE) cells. Biochemistry 30:6167-6174; 1991a.