On the Purification of l-Ornithine Decarboxylase from Rat Prostate and Effects of Thiol Compounds on the Enzyme

The activity and stability of l -ornithine decarboxylase from rat ventral prostate is markedly increased by certain thiol compounds, notably dithiothreitol. The enzyme was purified about 300-fold. Many properties of the purified enzyme are described. In the absence of added thiol compounds, the puri...

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Bibliographic Details
Published in:The Journal of biological chemistry 1971-03, Vol.246 (6), p.1725-1732
Main Authors: J. Jänne, H. G. Williams-Ashman, With the technical assistance of Mary E. Geroch
Format: Article
Language:English
Subjects:
Alcohols
Animals
Carboxy-Lyases - isolation & purification
Centrifugation, Density Gradient
Chromatography, Gel
Drug Stability
Electrophoresis, Disc
Enzyme Activation
Female
Hydrogen-Ion Concentration
Male
Ornithine
Polymers
Prostate - enzymology
Rats
Sulfhydryl Compounds
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Summary:The activity and stability of l -ornithine decarboxylase from rat ventral prostate is markedly increased by certain thiol compounds, notably dithiothreitol. The enzyme was purified about 300-fold. Many properties of the purified enzyme are described. In the absence of added thiol compounds, the purified ornithine decarboxylase apparently undergoes polymerization, as evidenced by its behavior on sucrose density gradients and in molecular sieving experiments. The larger forms of the enzyme appear to be catalytically inert, but can be reactivated by a number of sulfhydryl compounds, certain dithiols being superior to a number of monothiols in this respect.
ISSN:0021-9258
1083-351X
DOI:10.1016/s0021-9258(18)62370-1