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. 1978 Jul 15;174(1):283–290. doi: 10.1042/bj1740283

A protein-glucan intermediate during paramylon synthesis.

A D Tomos, D H Northcote
PMCID: PMC1185908  PMID: 100105

Abstract

A sodium deoxycholate extract containing glucosyltransferase activity was obtained from a particulate preparation from Euglena gracilis. It transferred glucose from UDP-[14C]glucose into material that was precipitated by trichloroacetic acid. This material released beta-(1 leads to 3)-glucan oligosaccharides into solution on incubation with weak acid, weak alkali and beta-(1 leads to 3)-glucosidase. The products of the incubation of the deoxycholate extract with UDP-[14C]glucose were analysed by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. Radioactive bands were obtained that had the properties of beta-(1 leads to 3)-glucan covalently linked to protein by a bond labile to weak acid. High-molecular-weight material containing a beta-(1 leads to 3)-glucan was also shown to be present by gel filtration. The bond linking glucan to aglycone is possibly a pyrophosphate linkage. It is proposed that in Euglena gracilis beta-(1 leads to 3)-glucan (paramylon) is synthesized on a protein primer.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. BANDURSKI R. S., AXELROD B. The chromatographic identification of some biologically important phosphate esters. J Biol Chem. 1951 Nov;193(1):405–410. [PubMed] [Google Scholar]
  2. Barengo R., Flawia M., Krisman C. R. The initiation of glycogen biosynthesis in Escherichia coli. FEBS Lett. 1975 May 15;53(3):274–278. doi: 10.1016/0014-5793(75)80035-4. [DOI] [PubMed] [Google Scholar]
  3. Berthillier G., Azzar G. J., Got R. Etude de l'activité de transfert de glucose, à partir d'UDP-glucose, dans les membranes microsomiques des hépatocytes de rat. Eur J Biochem. 1975 Feb 3;51(1):275–282. doi: 10.1111/j.1432-1033.1975.tb03927.x. [DOI] [PubMed] [Google Scholar]
  4. Clark A. F., Villemez C. L. The Formation of beta, 1 --> 4 Glucan from UDP-alpha-d-Glucose Catalyzed by a Phaseolus aureus Enzyme. Plant Physiol. 1972 Sep;50(3):371–374. doi: 10.1104/pp.50.3.371. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Elbein A. D. Biosynthesis of a cell wall glucomannan in mung bean seedlings. J Biol Chem. 1969 Mar 25;244(6):1608–1616. [PubMed] [Google Scholar]
  6. Fairbanks G., Steck T. L., Wallach D. F. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry. 1971 Jun 22;10(13):2606–2617. doi: 10.1021/bi00789a030. [DOI] [PubMed] [Google Scholar]
  7. Gahan L. C., Conrad H. E. An enzyme system for de novo biosynthesis of glycogen in Aerobacter aerogenes. Biochemistry. 1968 Nov;7(11):3979–3990. doi: 10.1021/bi00851a027. [DOI] [PubMed] [Google Scholar]
  8. Green J. R., Northcote D. H. The structure and function of glycoproteins synthesized during slime-polysaccharide production by membranes of the root-cap cells of maize (Zea mays). Biochem J. 1978 Mar 15;170(3):599–608. doi: 10.1042/bj1700599. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Harris P. J., Northcote D. H. Patterns of polysaccharide biosynthesis in differentiating cells of maize root-tips. Biochem J. 1970 Dec;120(3):479–491. doi: 10.1042/bj1200479. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Krisman C. R. A possible intermediate in the initiation of glycogen biosynthesis. Ann N Y Acad Sci. 1973 Feb 9;210:81–89. doi: 10.1111/j.1749-6632.1973.tb47563.x. [DOI] [PubMed] [Google Scholar]
  11. Krisman C. R. A possible intermediate in the initiation of glycogen biosynthesis. Biochem Biophys Res Commun. 1972 Feb 16;46(3):1206–1212. doi: 10.1016/s0006-291x(72)80103-7. [DOI] [PubMed] [Google Scholar]
  12. Krisman C. R., Barengo R. A precursor of glycogen biosynthesis: alpha-1,4-glucan-protein. Eur J Biochem. 1975 Mar 3;52(1):117–123. doi: 10.1111/j.1432-1033.1975.tb03979.x. [DOI] [PubMed] [Google Scholar]
  13. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  14. Lavintman N., Cardini C. E. Particulate UDP-glucose: Protein transglucosylase from potato tuber. FEBS Lett. 1973 Jan 1;29(1):43–46. doi: 10.1016/0014-5793(73)80011-0. [DOI] [PubMed] [Google Scholar]
  15. Lavintman N., Tandecarz J., Carceller M., Mendiara S., Cardini C. E. Role of uridine diphosphate glucose in the biosynthesis of starch. Mechanism of formation and enlargement of a glucoproteic acceptor. Eur J Biochem. 1974 Dec 16;50(1):145–155. doi: 10.1111/j.1432-1033.1974.tb03882.x. [DOI] [PubMed] [Google Scholar]
  16. MARECHAL L. R., GOLDEMBERG S. H. URIDINE DIPHOSPHATE GLUCOSE-BETA-1,3-GLUCAN BETA-3-GLUCOSYLTRANSFERASE FROM EUGLENA GRACILIS. J Biol Chem. 1964 Oct;239:3163–3167. [PubMed] [Google Scholar]
  17. OLAITAN S. A., NORTHCOTE D. H. Polysaccharides of Chlorella pyrenoidosa. Biochem J. 1962 Mar;82:509–519. doi: 10.1042/bj0820509. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. PATTERSON M. S., GREENE R. C. MEASUREMENT OF LOW ENERGY BETA-EMITTERS IN AQUEOUS SOLUTION BY LIQUID SCINTILLATION COUNTING OF EMULSIONS. Anal Chem. 1965 Jun;37:854–857. doi: 10.1021/ac60226a017. [DOI] [PubMed] [Google Scholar]
  19. TREVELYAN W. E., PROCTER D. P., HARRISON J. S. Detection of sugars on paper chromatograms. Nature. 1950 Sep 9;166(4219):444–445. doi: 10.1038/166444b0. [DOI] [PubMed] [Google Scholar]
  20. Tandecarz J., Lavintman N., Cardini C. E. Biosynthesis of starch. Formation of a glucoproteic acceptor by a potato non-sedimentable preparation. Biochim Biophys Acta. 1975 Aug 13;399(2):345–355. [PubMed] [Google Scholar]

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