title: Ornithine decarboxylase from Tetrahymena thermophila: purification, reversible modification and multiple forms.
abstract: T. thermophila ornithine decarboxylase was purified 1100-fold by an improved procedure to a specific activity of 2.31 x 10(4) nmol/hr/mg protein with a 28% yield. The purified enzyme was a monomer of Mr = 68,000 and had two isoelectric forms with pl's of 5.14 and 5.17 respectively. The Mr = 68,000 enzyme was reversibly modified by a cellular factor of approx. Mr = 10,000 to give rise to two additional forms with decreased DEAE-cellulose affinity.
mesh_terms: D000818:Animals; D002852:Chromatography, Ion Exchange; D007526:Isoelectric Point; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism; D008970:Molecular Weight; D009955:Ornithine Decarboxylase / Q000302:isolation & purification* / Q000378:metabolism; D013768:Tetrahymena / Q000201:enzymology*
chemical_list: D007527:Isoenzymes; D009955:Ornithine Decarboxylase