Purification and properties of ornithine decarboxylase from Lactobacillus sp. 30a.
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منابع مشابه
Purification and Properties of Ornithine Decarboxylase
Ornithine decarboxylase was purified to homogeneity, as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and polyacrylamide gel electrofocusing, about 710,000-fold with a 35% yield from the liver cytosol of thioacetamide-treated rats. The final specific activity was approximately 24,400 nmol/ min/mg of protein. The apparent molecular weight of the enzyme determined by gel fil...
متن کاملPurification and Properties of Ornithine Decarboxylase
Inducible ornithine decarboxylase from Lactobacillus sp. 30a has been purified to homogeneity as judged by ultracentrifugation and gel electrophoresis. Unlike histidine decarboxylase from the same species (a pyruvoyl enzyme), ornithine decarboxylase is a pyridoxal phosphate enzyme. The purified enzyme is specific for Lornithine (Km 1.7 m ~ ; specific activity, 150 to 200 pmol min” mg” at 37°C) ...
متن کاملPurification and properties of ornithine decarboxylase from Physarum polycephalum.
Ornithine decarboxylase (EC 4.1.1.17) has been purified 3,500-fold from the plasmodia of Physarum polycephalum. The purified material exhibited a Km for ornithine of 0.6 mM and Vmax of 20 mumol of CO2 formed per min/mg at 30 degrees C (62 mumol/min/mg at 37 degrees C). It migrated as a single protein and activity species on high pressure liquid chromatography (TSK-3000) in 0.15 M NaCl (Mr = 80,...
متن کاملThree-component lysine/ornithine decarboxylation system in Lactobacillus saerimneri 30a.
Lactic acid bacteria play a pivotal role in many food fermentations and sometimes represent a health threat due to the ability of some strains to produce biogenic amines that accumulate in foods and cause trouble following ingestion. These strains carry specific enzymatic systems catalyzing the uptake of amino acid precursors (e.g., ornithine and lysine), the decarboxylation inside the cell, an...
متن کاملPurification and some properties of a protein inhibitor (antizyme) of ornithine decarboxylase from rat liver.
A protein inhibitor to ornithine decarboxylase, antizyme, was purified to homogeneity, as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, about 600,000-fold with a 15% yield from the liver cytosol of putrescine-treated rats. Antizyme was very labile but markedly stabilized in the presence of Tween 80 and 2-mercaptoethanol. The apparent molecular weight of antizyme was deter...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1980
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)70724-8