The role of glycosylation in storage-protein synthesis in developing pea seeds |
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Authors: | Jane Badenoch-Jones Donald Spencer T J V Higgins Adele Millerd |
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Institution: | (1) Division of Plant Industry, CSIRO, P.O. Box 1600, 2601 Canberra City, A.C.T., Australia;(2) Present address: Research School of Biological Sciences, Australian National University, P.O. Box 475, 2601 Canberra, A.C.T., Australia |
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Abstract: | Intact pea (Pisum sativum L.) cotyledons were incubated with 14C]glucosamine at several stages of seed development and the resultant radioactive proteins were analysed by gel electrophoresis combined with immunoaffinity chromatography and sucrose gradient fractionation. Glucosamine was incorporated into at least five vicilin polypeptides (approx. molecular weight 70,000; 50,000, two components; 14,000, two components). No incorporation was detected into the subunits of legumin. Tunicamycin at 50 g/ml largely inhibited glucosamine incorporation but had little effect on the incorporation of 14C-labelled amino acids into cotyledon proteins, including vicilin. The assembly of vicilin polypeptides into full-sized protein oligomers (7–9 S) was also unaffected by tunicamycin. Chromatography on concanavalin A confirmed that glycosylation of cotyledon proteins was inhibited by tunicamycin. It is concluded that glycosylation of most cotyledonary proteins involves lipid-linked sugar intermediates, but that glycosylation itself is not an essential step in the synthesis of vicilin polypeptides nor in their assembly into oligomers.Abbreviations IgG
immunoglobulin G
- M Wt
approximate molecular weight based on electrophoretic mobility relative to that of protein standards
- SDS-PAGE
Na-dodecyl sulfate-polyacrylamide gel electrophoresis |
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Keywords: | Glucosamine Glycoproteins Legumin Pisum (storage protein) Storage protein glycosylation Vicilin |
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