Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1977 Jan 15;162(1):201–203. doi: 10.1042/bj1620201

The turnover of hamster fibroblast lysosomal beta-D-glucuronidase.

M J Warburton, C H Wynn
PMCID: PMC1164585  PMID: 849277

Abstract

The half-life of hamster fibroblast beta-D-glucuronidase (EC 3.2.1.31) was estimated to be 4-5 days by measuring the decay with time of the radioactivity in beta-D-glucuronidase isolated from cells grown in the presence of 14C-labelled amino acids. A new affinity-chromatographic procedure for the purification of beta-D-glucuronidase is described.

Full text

PDF
201

Selected References

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

  1. Cuatrecasas P. Protein purification by affinity chromatography. Derivatizations of agarose and polyacrylamide beads. J Biol Chem. 1970 Jun;245(12):3059–3065. [PubMed] [Google Scholar]
  2. Dean R. T. Concerning a possible mechanism for selective capture of cytoplasmic proteins by lysosomes. Biochem Biophys Res Commun. 1975 Nov 17;67(2):604–609. doi: 10.1016/0006-291x(75)90855-4. [DOI] [PubMed] [Google Scholar]
  3. Goldberg A. L., Dice J. F. Intracellular protein degradation in mammalian and bacterial cells. Annu Rev Biochem. 1974;43(0):835–869. doi: 10.1146/annurev.bi.43.070174.004155. [DOI] [PubMed] [Google Scholar]
  4. Goldstone A., Koenig H. Synthesis and turnover of lysosomal glycoproteins. Relation to the molecular heterogeneity of the lysosomal enzymes. FEBS Lett. 1974 Feb 15;39(2):176–181. doi: 10.1016/0014-5793(74)80045-1. [DOI] [PubMed] [Google Scholar]
  5. Kanfer J. N., Mumford R. A., Raghavan S. S., Byrd J. Purification of beta-glucosidase activities from bovine spleen by affinity chromatography. Anal Biochem. 1974 Jul;60(1):200–205. doi: 10.1016/0003-2697(74)90145-6. [DOI] [PubMed] [Google Scholar]
  6. Kanfer J. N., Petrovich G., Mumford R. A. Purification of alpha- and beta-galactosidases by affinity chromatography. Anal Biochem. 1973 Sep;55(1):301–305. doi: 10.1016/0003-2697(73)90319-9. [DOI] [PubMed] [Google Scholar]
  7. LEVVY G. A. The preparation and properties of beta-glucuronidase. IV. Inhibition by sugar acids and their lactones. Biochem J. 1952 Nov;52(3):464–472. doi: 10.1042/bj0520464. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Pokorny M., Glaudemans C. P. Purification of N-acetyl beta-D-hexosaminidase from bull epididymis by affinity chromatography. FEBS Lett. 1975 Jan 15;50(1):66–69. doi: 10.1016/0014-5793(75)81042-8. [DOI] [PubMed] [Google Scholar]
  9. Segal H. I., Winkler J. R., Miyagi M. P. Relationship between digradation rates of proteins in vivo and their susceptibility to lysosomal proteases. J Biol Chem. 1974 Oct 10;249(19):6364–6365. [PubMed] [Google Scholar]
  10. Wang C-C, Touster O. Turnover studies on proteins of rat liver lysosomes. J Biol Chem. 1975 Jul 10;250(13):4896–4902. [PubMed] [Google Scholar]
  11. Warburton M. J., Wynn C. H. Characterisation of the lysosomal heterogeneity in Chinese-hamster fibroblasts. Eur J Biochem. 1976 Jun 1;65(2):341–348. doi: 10.1111/j.1432-1033.1976.tb10347.x. [DOI] [PubMed] [Google Scholar]
  12. Warburton M. J., Wynn C. H. The effect of intralysosomal sucrose storage on the turnover of hamster fibroblast lysosomal and Golgi-apparatus enzymes. Biochem J. 1976 Aug 15;158(2):401–407. doi: 10.1042/bj1580401. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Warburton M. J., Wynn C. H. The hyperactivity of hamster fibroblast lysosomal enzymes after endocytosis of sucrose. Biochem Biophys Res Commun. 1976 May 3;70(1):94–100. doi: 10.1016/0006-291x(76)91113-x. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES