Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1978 Mar 1;169(3):709–712. doi: 10.1042/bj1690709

Rapid and convenient method for the assay of aminopropyltransferases.

H Hibasami, A E Pegg
PMCID: PMC1183845  PMID: 646794

Abstract

A new method for the assay of aminopropyltransferase activity is described. The method measures the formation of [methyl-14C]methylthioadenosine from decarboxylated S-adenosyl[methyl-14C]methionine in the presence of an amine acceptor. When used with extracts from rat ventral prostate, kidney, liver or brain, and with putrescine or spermidine as amines, the method gave results in excellent agreement with those obtained by the much more time-consuming conventional method. It was found that 1,3-diamino-propane and 1,8-diamino-octane were not acceptors for the prostatic enzyme fraction, but 1,5-diaminopentane (cadaverine) was active and 1,9-diaminononane and 1,12-diaminododecane also lead to the production of [methyl-14C]methylthioadenosine.

Full text

PDF
709

Selected References

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

  1. Bowman W. H., Tabor C. W., Tabor H. Spermidine biosynthesis. Purification and properties of propylamine transferase from Escherichia coli. J Biol Chem. 1973 Apr 10;248(7):2480–2486. [PubMed] [Google Scholar]
  2. Guha S. K., Jänne J. Inhibition of ornithine decarboxylase in vivo in rat ovary. Biochem Biophys Res Commun. 1977 Mar 7;75(1):136–142. doi: 10.1016/0006-291x(77)91300-6. [DOI] [PubMed] [Google Scholar]
  3. Hannonen P., Jänne J., Raina A. Separation and partial purification of S-adenosylmethionine decarboxylase and spermidine and spermine synthases from rat liver. Biochem Biophys Res Commun. 1972 Jan 31;46(2):341–348. doi: 10.1016/s0006-291x(72)80144-x. [DOI] [PubMed] [Google Scholar]
  4. Jänne J., Schenone A., Williams-Ashman H. G. Separation of two proteins required for synthesis of spermidine from S-adenosyl-L-methionine and putrescine in rat prostate. Biochem Biophys Res Commun. 1971 Feb 19;42(4):758–764. doi: 10.1016/0006-291x(71)90552-3. [DOI] [PubMed] [Google Scholar]
  5. Jänne J., Williams-Ashman H. G. Dissociation of putrescine-activated decarboxylation of S-adenosyl-L-methionine from the enzymic synthesis of spermidine and spermine by purified prostatic enzyme preparations. Biochem Biophys Res Commun. 1971 Jan 22;42(2):222–229. [PubMed] [Google Scholar]
  6. Kallio A., Pösö H., Guha S. K., Jänne J. Polyamines and their biosynthetic enzymes in Ehrlich ascites-carcinoma cells. Modification of tumour polyamine pattern by diamines. Biochem J. 1977 Jul 15;166(1):89–94. doi: 10.1042/bj1660089. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Kallio A., Pösö H., Scalabrino G., Jänne J. Regulation of ornithine decarboxylase by diamines in regenerating rat liver. FEBS Lett. 1977 Feb 1;73(2):229–234. doi: 10.1016/0014-5793(77)80987-3. [DOI] [PubMed] [Google Scholar]
  8. 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]
  9. Pegg A. E., Williams-Ashman H. G. Enzymic synthesis of spermine in rat prostate. Arch Biochem Biophys. 1970 Mar;137(1):156–165. doi: 10.1016/0003-9861(70)90422-4. [DOI] [PubMed] [Google Scholar]
  10. Pegg A. E., Williams-Ashman H. G. On the role of S-adenosyl-L-methionine in the biosynthesis of spermidine by rat prostate. J Biol Chem. 1969 Feb 25;244(4):682–693. [PubMed] [Google Scholar]
  11. Pegg A. E., Williams-Ashman H. G. Phosphate-stimulated breakdown of 5'-methylthioadenosine by rat ventral prostate. Biochem J. 1969 Nov;115(2):241–247. doi: 10.1042/bj1150241. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Pöso H., Jänne J. Inhibition of ornithine decarboxylase activity and spermidine accumulation in regenerating rat liver. Biochem Biophys Res Commun. 1976 Apr 19;69(4):885–892. doi: 10.1016/0006-291x(76)90456-3. [DOI] [PubMed] [Google Scholar]
  13. Raina A., Jänne J. Physiology of the natural polyamines putrescine, spermidine and spermine. Med Biol. 1975 Jun;53(3):121–147. [PubMed] [Google Scholar]
  14. Raina Aarne, Hannonen Pekka. Separation of enzyme activities catalysing spermidine and spermine synthesis in rat brain. FEBS Lett. 1971 Jul 15;16(1):1–4. doi: 10.1016/0014-5793(71)80669-5. [DOI] [PubMed] [Google Scholar]
  15. Tabor C. W., Tabor H. 1,4-Diaminobutane (putrescine), spermidine, and spermine. Annu Rev Biochem. 1976;45:285–306. doi: 10.1146/annurev.bi.45.070176.001441. [DOI] [PubMed] [Google Scholar]
  16. Tabor H., Tabor C. W. Biosynthesis and metabolism of 1,4-diaminobutane, spermidine, spermine, and related amines. Adv Enzymol Relat Areas Mol Biol. 1972;36:203–268. doi: 10.1002/9780470122815.ch7. [DOI] [PubMed] [Google Scholar]

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

RESOURCES