Histamine N-methyltransferase (EC 22.214.171.124) 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.
Research Article|February 01 1986
Purification and kinetic properties of ox brain histamine N-methyltransferase
Biochem J (1986) 233 (3): 669-676.
- Views Icon Views
- PDF LinkPDF
- Share Icon Share
- Cite Icon Cite
W L Gitomer, K F Tipton; Purification and kinetic properties of ox brain histamine N-methyltransferase. Biochem J 1 February 1986; 233 (3): 669–676. doi: https://doi.org/10.1042/bj2330669
Download citation file: