Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1986 Feb 1;233(3):669–676. doi: 10.1042/bj2330669

Purification and kinetic properties of ox brain histamine N-methyltransferase.

W L Gitomer, K F Tipton
PMCID: PMC1153084  PMID: 3707517

Abstract

Histamine N-methyltransferase (EC 2.1.1.8) was purified 1100-fold from ox brain. The native enzyme has an Mr of 34800 +/- 2400 as measured by gel filtration on Sephadex G-100. The enzyme is highly specific for histamine. It does not methylate noradrenaline, adrenaline, DL-3,4-dihydroxymandelic acid, 3,4-dihydroxyphenylacetic acid, 3-hydroxytyramine or imidazole-4-acetic acid. Unlike the enzyme from rat and mouse brain, ox brain histamine N-methyltransferase did not exhibit substrate inhibition by histamine. Initial rate and product inhibition studies were consistent with an ordered steady-state mechanism with S-adenosylmethionine being the first substrate to bind to the enzyme and N-methylhistamine being the first product to dissociate.

Full text

PDF
669

Selected References

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

  1. Andrews P. The gel-filtration behaviour of proteins related to their molecular weights over a wide range. Biochem J. 1965 Sep;96(3):595–606. doi: 10.1042/bj0960595. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Aures D., Fleming R., Håkanson R. Separation and detection of biogenic amines by thin-layer chromatography. Micro-analysis of tissue amines and of enzymes involved in their metabolism. J Chromatogr. 1968 Mar 19;33(3):480–493. doi: 10.1016/s0021-9673(00)98677-1. [DOI] [PubMed] [Google Scholar]
  3. BROWN D. D., TOMCHICK R., AXELROD J. The distribution and properties of a histamine-methylating enzyme. J Biol Chem. 1959 Nov;234:2948–2950. [PubMed] [Google Scholar]
  4. Baudry M., Chast F., Schwartz J. C. Studies on S-adenosylhomocysteine inhibition of histamine transmethylation in brain. J Neurochem. 1973 Jan;20(1):13–21. doi: 10.1111/j.1471-4159.1973.tb12099.x. [DOI] [PubMed] [Google Scholar]
  5. Bowsher R. R., Verburg K. M., Henry D. P. Rat histamine N-methyltransferase. Quantification, tissue distribution, purification, and immunologic properties. J Biol Chem. 1983 Oct 25;258(20):12215–12220. [PubMed] [Google Scholar]
  6. Cornish-Bowden A., Eisenthal R. Statistical considerations in the estimation of enzyme kinetic parameters by the direct linear plot andother methods. Biochem J. 1974 Jun;139(3):721–730. doi: 10.1042/bj1390721. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  8. Eisenthal R., Cornish-Bowden A. The direct linear plot. A new graphical procedure for estimating enzyme kinetic parameters. Biochem J. 1974 Jun;139(3):715–720. doi: 10.1042/bj1390715. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. 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]
  10. Francis D. M., Thompson M. F., Greaves M. W. The kinetic properties and reaction mechanism of histamine methyltransferase from human skin. Biochem J. 1980 Jun 1;187(3):819–828. doi: 10.1042/bj1870819. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Gulliver P. A., Tipton K. F. Direct extraction radioassay for catechol-Q-methyl-transferase activity. Biochem Pharmacol. 1978 Mar 1;27(5):773–775. doi: 10.1016/0006-2952(78)90519-1. [DOI] [PubMed] [Google Scholar]
  12. ITZHAKI R. F., GILL D. M. A MICRO-BIURET METHOD FOR ESTIMATING PROTEINS. Anal Biochem. 1964 Dec;9:401–410. doi: 10.1016/0003-2697(64)90200-3. [DOI] [PubMed] [Google Scholar]
  13. Matuszewska B., Borchardt R. T. Guinea pig brain histamine N-methyltransferase: purification and partial characterization. J Neurochem. 1983 Jul;41(1):113–118. doi: 10.1111/j.1471-4159.1983.tb11821.x. [DOI] [PubMed] [Google Scholar]
  14. Mudd S. H., Poole J. R. Labile methyl balances for normal humans on various dietary regimens. Metabolism. 1975 Jun;24(6):721–735. doi: 10.1016/0026-0495(75)90040-2. [DOI] [PubMed] [Google Scholar]
  15. Orr E. L., Quay W. B. Product inhibition of rat brain histamine-N-methyltransferase. J Neurochem. 1978 Jun;30(6):1539–1542. doi: 10.1111/j.1471-4159.1978.tb10490.x. [DOI] [PubMed] [Google Scholar]
  16. SCHAYER R. W. Catabolism of physiological quantities of histamine in vivo. Physiol Rev. 1959 Jan;39(1):116–126. doi: 10.1152/physrev.1959.39.1.116. [DOI] [PubMed] [Google Scholar]
  17. Saavedra J. M. The role of methylating enzymes in brain function. Essays Neurochem Neuropharmacol. 1977;1:1–41. [PubMed] [Google Scholar]
  18. Sellinger O. Z., Schatz R. A., Ohlsson W. G. Rat and mouse brain histamine N-methyltransferase: modulation by methylated indoleamines. J Neurochem. 1978 Feb;30(2):437–445. doi: 10.1111/j.1471-4159.1978.tb06548.x. [DOI] [PubMed] [Google Scholar]
  19. Taylor K. M., Snyder S. H. Histamine methyltransferase: inhibition and potentiation by antihistamines. Mol Pharmacol. 1972 May;8(3):300–310. [PubMed] [Google Scholar]
  20. Taylor K. M., Snyder S. H. Isotopic microassay of histamine, histidine, histidine decarboxylase and histamine methyltransferase in brain tissue. J Neurochem. 1972 May;19(5):1343–1358. doi: 10.1111/j.1471-4159.1972.tb01459.x. [DOI] [PubMed] [Google Scholar]
  21. Thithapandha A., Cohn V. H. Brain histamine N-methyltransferase purification, mechanism of action, and inhibition by drugs. Biochem Pharmacol. 1978 Feb 1;27(3):263–271. doi: 10.1016/0006-2952(78)90227-7. [DOI] [PubMed] [Google Scholar]
  22. Zappia V., Galletti P., Cartenì-Farina M., Servillo L. A coupled spectrophotometric enzyme assay for methyltransferases. Anal Biochem. 1974 Mar;58(1):130–138. doi: 10.1016/0003-2697(74)90449-7. [DOI] [PubMed] [Google Scholar]

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

RESOURCES