Full-size form of human liver AMP-deaminase?

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 po...

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Published inMolecular and cellular biochemistry Vol. 266; no. 1-2; pp. 133 - 137
Main Authors Szydlowska, M, Chodorowski, Z, Rybakowska, I, Nagel-Starczynowska, G, Kaletha, K
Format Journal Article
LanguageEnglish
Published Netherlands Springer Nature B.V 01.11.2004
Subjects
AMP Deaminase - chemistry
AMP Deaminase - isolation & purification
Chromatography, Liquid
Electrophoresis, Polyacrylamide Gel
Humans
Isoenzymes - chemistry
Isoenzymes - isolation & purification
Liver - enzymology
Molecular Weight
Proteins
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Summary: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.
Bibliography:ObjectType-Article-1
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content type line 23
ISSN:0300-8177
1573-4919
DOI:10.1023/b:mcbi.0000049150.19623.e8