PMID: 3753469Jun 1, 1986Paper

Purification of mouse brain ornithine decarboxylase reveals its presence as an inactive complex with antizyme

The Biochemical Journal
P H LaitinenA E Pajunen

Abstract

Mouse brain ornithine decarboxylase (ODC) was purified to near-homogeneity by using (NH4)2SO4 precipitation and chromatography on heparin-Sepharose, pyridoxamine phosphate-agarose and DEAE-cellulose. On SDS/polyacrylamide-gel electrophoresis, the final preparation gave one protein band similar to that obtained for purified mouse kidney enzyme, corresponding to an Mr of 53.000. The overall yield of the purification exceeded about 50-fold the total activity of the enzyme in the starting material. By affinity chromatography on ODC-bound Sepharose, the extra enzyme activity was shown to originate, at least partly, from the enzyme-antizyme complex. These results demonstrate that ODC in mouse brain occurs mainly in an inactive form and is activated during purification.

Citations

Mar 27, 2016·Pharmacological Research : the Official Journal of the Italian Pharmacological Society·Gustavo Petri GuerraCarlos Fernando Mello
Dec 4, 2009·Amino Acids·Andrés J López-ContrerasRafael Peñafiel
Dec 5, 2000·Journal of Neuroscience Research·P KilpeläinenM Pelto-Huikko
Oct 12, 2018·Medical Sciences : Open Access Journal·Bruno Ramos-MolinaRafael Peñafiel
Jan 1, 1988·Preparative Biochemistry·M NishiyamaS Hayashi
Sep 3, 1999·The Journal of Biological Chemistry·C ZhuP Coffino
Dec 1, 1995·Progress in Neurobiology·R A Kauppinen, L I Alhonen
Jan 19, 1990·Biochimica Et Biophysica Acta·J L Mitchell, H J Chen
Jan 1, 1991·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·T G Baby, S Hayashi

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