The glycoprotein 71 of ecotropic Friend murine leukemia virus. Structure of the oligosaccharides linked to asparagine-12 |
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| Authors: | M Schlüter D Linder R Geyer G Hunsmann J Schneider S Stirm |
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| Affiliation: | 1. Biochemisches Institut am Klinikum der Universität, friedrichstrasse 24, D-6300 Giessen FRG;2. Forschergruppe Tumorimmunologie, Stefan Meier-Str. 8, D-7800 Freiburg, FRG |
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| Abstract: | The glycoprotein from Friend murine leukemia virus was digested with protease from Staphylococcus aureus V8. A glycopeptide comprising the N-terminal glycosylation site (Asn-12) was isolated from the mixture of fragments and analyzed by amino acid sequencing and methylation-capillary gas chromatography-mass spectrometry before and after treatment with sialidase from Vibrio cholerae. Asn-12 was thus found to be substituted by a family of partially sialylated, fucosylated, and intersected glycoprotein N-glycans of the hybrid type. |
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| Keywords: | Glycoprotein Glycosylation site Leukemia Methylation analysis Oligosaccharide structure Retrovirus GC, gas chromatography gp, glycoprotein HPLC, high-performance liquid chromatography rHPLC, reversed-phase HPLC MS, mass spectrometry MuLV, murine leukemia virus F-MuLV, Friend strain of MuLV PTH amino acids, phenylthiohydantoin amino acids SA, sialic acid |
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