The High Mannose Oligosaccharide of Phytohemagglutinin Is Attached to Asparagine 12 and the Modified Oligosaccharide to Asparagine 60
- 1 May 1986
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 81 (1) , 320-322
- https://doi.org/10.1104/pp.81.1.320
Abstract
Phytohemagglutinin, the lectin of the common bean Phaseolus vulgaris, has a high mannose and a modified (fucosylated) oligosaccharide on each polypeptide. Fractionation by high performance liquid chromatography of tryptic digests of [3H]fucose or [3H]glucosamine labeled phytohemagglutinin, followed by amino acid sequencing of the isolated glycopeptides, shows that the high mannose oligosaccharide is attached to Asn12 and the modified oligosaccharide to Asn60 of the protein. In animal glycoproteins, high mannose chains are rarely found at the N-terminal side of complex chains.This publication has 10 references indexed in Scilit:
- Characterization of two Phaseolus vulgaris phytohemagglutinin genes closely linked on the chromosome.The EMBO Journal, 1985
- Transient N-acetylglucosamine in the biosynthesis of phytohemagglutinin: attachment in the Golgi apparatus and removal in protein bodies.The Journal of cell biology, 1984
- Phaseolus vulgaris phytohemagglutinin contains high-mannose and modified oligosaccharide chainsPlanta, 1984
- Correlation of glycosylation forms with position in amino acid sequenceThe Journal of cell biology, 1983
- The Golgi apparatus mediates the transport of phytohemagglutinin to the protein bodies in bean cotyledonsPlanta, 1983
- Host-dependent variation of asparagine-linked oligosaccharides at individual glycosylation sites of Sindbis virus glycoproteins.Journal of Biological Chemistry, 1983
- [43] Analysis of phenylthiohydantoins by ultrasensitive gradient high-performance liquid chromatographyPublished by Elsevier ,1983
- A gas-liquid solid phase peptide and protein sequenator.Journal of Biological Chemistry, 1981
- Pulse-labeling Studies on Protein Synthesis in Developing Pea Seeds and Evidence of a Precursor Form of Legumin Small SubunitPlant Physiology, 1980