Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
|
pubmed:dateCreated |
1983-7-15
|
pubmed:abstractText |
Ornithine decarboxylase was purified from kidneys of androgen-treated mice to a greater than 95% purity. Two-dimensional gel electrophoresis revealed charge heterogeneity in the enzyme (pI 4.7-4.9) which was observed both by protein staining and by covalent labeling with [3H]alpha-difluoromethylornithine. Antibodies raised in rabbits inhibited the activity of the enzyme, formed a single rocket in crossed immunoelectrophoresis, and bound [3H]alpha-difluoromethylornithine-labeled enzyme as well as [125I]iodoornithine decarboxylase. A sensitive radioimmunoassay for the enzyme was established; the minimal detectable enzyme concentration was 0.1 ng/assay tube that corresponded to about 0.1-0.2 ng/mg of cytosol protein. The antiserum cross-reacted with enzymes from different tissues from mouse, rat, hamster, and human. Immunoreactive ornithine decarboxylase concentration in renal cytosol of male mice was 13-fold higher than that in the females (36.2 +/- 2.7 versus 2.8 +/- 0.2 ng/mg of cytosol protein; mean +/- S.E.); treatment with testosterone implants for 5-7 days increased the concentration to 522 +/- 66 ng/mg of protein. After administration of a single dose of testosterone (10 mg) to female mice, an increased immunoreactive ornithine decarboxylase concentration was detected as soon as 2 h, and rose sharply between 8 and 24 h after steroid administration. These changes were similar to those seen by assays of the catalytically active enzyme. The half-life of immunoreactive ornithine decarboxylase in mouse kidney, as measured after inhibition of protein synthesis in vivo by cycloheximide administration, was 16 min in nontreated and 140 min in androgen-treated male animals, while the corresponding values for the catalytically active enzyme were 9 and 90 min.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigen-Antibody Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Carboxy-Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/Drug Implants,
http://linkedlifedata.com/resource/pubmed/chemical/Immune Sera,
http://linkedlifedata.com/resource/pubmed/chemical/Ornithine Decarboxylase,
http://linkedlifedata.com/resource/pubmed/chemical/Testosterone
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0021-9258
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
10
|
pubmed:volume |
258
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
6735-40
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:6853503-Animals,
pubmed-meshheading:6853503-Antigen-Antibody Complex,
pubmed-meshheading:6853503-Carboxy-Lyases,
pubmed-meshheading:6853503-Cytosol,
pubmed-meshheading:6853503-Drug Implants,
pubmed-meshheading:6853503-Female,
pubmed-meshheading:6853503-Immune Sera,
pubmed-meshheading:6853503-Kidney,
pubmed-meshheading:6853503-Kinetics,
pubmed-meshheading:6853503-Mice,
pubmed-meshheading:6853503-Ornithine Decarboxylase,
pubmed-meshheading:6853503-Testosterone
|
pubmed:year |
1983
|
pubmed:articleTitle |
Ornithine decarboxylase in mouse kidney. Purification, characterization, and radioimmunological determination of the enzyme protein.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|