ArticleMolecular and cellular biochemistry2004
Full-size form of human liver AMP-deaminase?
Article in Molecular and cellular biochemistry, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 14 citations in OpenAlex.
- Isozymes of AMP-Deaminase in Muscles Myasthenia Gravis Patients.International journal of peptide research and therapeutics · 2016Article
- AMP-deaminase from goldfish white muscle: regulatory properties and redistribution under exposure to high environmental oxygen level.Fish physiology and biochemistry · 2009Article
- Expression patterns of AMP-deaminase isozymes in human hepatocellular carcinoma (HCC).Molecular and cellular biochemistry · 2008Article
- Regulation of 5'-adenosine monophosphate deaminase in the freeze tolerant wood frog, Rana sylvatica.BMC biochemistry · 2008Article
- AMP-deaminase from normal and cirrhotic human liver: a comparative study.Molecular and cellular biochemistry · 2004Article
- Human liver AMP-deaminase--oligomeric forms of the enzyme.Molecular and cellular biochemistry · 2002Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
AMP-deaminase from human liver was purified by two-step phosphocellulose chromatography, and SDS-PAG electrophoresis of the most active enzyme fraction eluted has been performed. The largest of the protein fragments revealed had a size (92 kDa) of an apparent full-size enzyme subunit, and reacted positively with antibodies produced against specific human ampd2 gene product. Three-day storage at cold room temperature modified significantly the electrophoretical pattern of the enzyme, evidencing continuous and progressive degradation of its structure. This is a first report evidencing the presence of apparent full-size form of human liver AMP-deaminase in preparation obtained from endogenous source.
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Registered trials
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