Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1977 May 15;164(2):461–464. doi: 10.1042/bj1640461

Enhanced plasma persistence of therapeutic enzymes by coupling to soluble dextran.

R F Sherwood, J K Baird, T Atkinson, C N Wiblin, D A Rutter, D C Ellwood
PMCID: PMC1164813  PMID: 880251

Abstract

Conjugation of carboxypeptidase G and arginase, two enzymes of therapeutic interest, to a soluble dextran significantly enhanced plasma persistence in normal and tumour-bearing mice. A prolonged decrease in arginine concentrations in plasma of tumour-bearing mice was demonstrated by using the dextran-linked arginase. Gel filtration of dextran-enzyme conjugate showed that enzyme activity co-chromatographed as a single peak with carbohydrate, and enzyme was shown to be covalently linked to the dextran.

Full text

PDF
461

Selected References

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

  1. Chou T. C., Handschumacher R. E. Production of L-asparagine by tumor cells and the effect of asparagine analogs. Biochem Pharmacol. 1972 Jan;21(1):39–48. doi: 10.1016/0006-2952(72)90248-1. [DOI] [PubMed] [Google Scholar]
  2. Holcenberg J. S., Schmer G., Teller D. C. Biologic and physical properties of succinylated and glycosylated Acinetobacter glutaminase-asparaginase. J Biol Chem. 1975 Jun 10;250(11):4165–4170. [PubMed] [Google Scholar]
  3. Kågedal L., Akerström S. Binding of covalent proteins to polysaccharides by cyanogen bromide and organic cyanates. I. Preparation of soluble glycine-, insulin- and ampicillin-dextran. Acta Chem Scand. 1971;25(5):1855–1859. doi: 10.3891/acta.chem.scand.25-1855. [DOI] [PubMed] [Google Scholar]
  4. 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]
  5. McCullough J. L., Chabner B. A., Bertino J. R. Purification and properties of carboxypeptidase G 1 . J Biol Chem. 1971 Dec 10;246(23):7207–7213. [PubMed] [Google Scholar]
  6. Neerunjun E. D., Gregoriadis G. Tumour regression with liposome-entrapped asparaginase: some immunological advantages. Biochem Soc Trans. 1976;4(1):133–134. doi: 10.1042/bst0040133. [DOI] [PubMed] [Google Scholar]
  7. Riley V., Campbell H. A., Stock C. C. Asparaginase clearance: influence of the LDH-elevating virus. Proc Soc Exp Biol Med. 1970 Jan;133(1):38–42. doi: 10.3181/00379727-133-34402. [DOI] [PubMed] [Google Scholar]
  8. Riley V., Spackman D., Fitzmaurice M. A., Roberts J., Holcenberg J. S., Dolowy W. C. Therapeutic properties of a new glutaminase-asparaginase preparation and the influence of the lactate dehydrogenase-elevating virus. Cancer Res. 1974 Feb;34(2):429–438. [PubMed] [Google Scholar]
  9. Teien A. N., Odegård R., Christensen T. B. Heparin coupled to albumin, dextran and ficoll: influence on blood coagulation and platelets, and in vivo duration. Thromb Res. 1975 Aug;7(2):273–284. doi: 10.1016/0049-3848(75)90186-3. [DOI] [PubMed] [Google Scholar]
  10. Updike S. J., Wakamiya R. T., Lightfoot E. N., Jr Asparaginase entrapped in red blood cells: action and survival. Science. 1976 Aug 20;193(4254):681–683. doi: 10.1126/science.821145. [DOI] [PubMed] [Google Scholar]
  11. Vegarud G., Christnsen T. B. Glycosylation of Proteins: a new method of enzyme stabilization. Biotechnol Bioeng. 1975 Sep;17(9):1391–1397. doi: 10.1002/bit.260170918. [DOI] [PubMed] [Google Scholar]
  12. WILSON J. S., ESTES E. H., Jr, DOYLE J. T., BLOOM W. L., WARREN J. V. The use of dextran in the treatment of blood loss and shock. Am J Med Sci. 1952 Apr;223(4):364–369. doi: 10.1097/00000441-195204000-00002. [DOI] [PubMed] [Google Scholar]

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

RESOURCES