Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1986-2-14
|
pubmed:abstractText |
An (ADP-ribose)n glycohydrolase has been purified more than 3,000-fold from guinea pig liver nuclei with an 18% yield. The glycohydrolase activity present in the nuclei was solubilized only by sonication at high ionic strength and purified by sequential chromatographic steps on phosphocellulose, DEAE-cellulose, Blue Sepharose, and single-stranded DNA cellulose. The purified protein exhibited one predominant protein band on sodium dodecyl sulfate-polyacrylamide gels with an estimated molecular weight of 75,500. On Sephadex G-100 gel filtration, single coincident peaks of (ADP-ribose)n glycohydrolase activity and protein with a molecular weight value of 72,000 were observed. The Km value for (ADP-ribose)n and the maximal velocity of the highly purified glycohydrolase were 2.3 microM and 36 mumol of ADP-ribose released from (ADP-ribose)n . min-1 . mg protein-1, respectively. Hydrolysis of (ADP-ribose)n by the enzyme was exoglycosidic in nature. The optimum pH for the enzyme activity was apparent at 6.8-7.0. Sulfhydryl compounds and monovalent cations were required for the maximal activity. The enzyme was sensitive to Ca2+ but not to Mg2+. The enzyme activity was inhibited by ADP-ribose, cyclic AMP (adenosine 3':5'-monophosphate) and diadenosine 5',5'''-p1,p4-tetraphosphate. Denatured DNA and histones were inhibitory, but native DNA and its histone complex were not inhibitory. Our data indicate that the glycohydrolase is present only as a minor protein in nuclei, being present in perhaps about 50,000 molecules/nucleus.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cations,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfhydryl Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/poly ADP-ribose glycohydrolase
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
0021-9258
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
261
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
965-9
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:3941108-Animals,
pubmed-meshheading:3941108-Cations,
pubmed-meshheading:3941108-Cell Nucleus,
pubmed-meshheading:3941108-Chromatography, DEAE-Cellulose,
pubmed-meshheading:3941108-Chromatography, Gel,
pubmed-meshheading:3941108-DNA,
pubmed-meshheading:3941108-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:3941108-Glycoside Hydrolases,
pubmed-meshheading:3941108-Guinea Pigs,
pubmed-meshheading:3941108-Histones,
pubmed-meshheading:3941108-Hydrogen-Ion Concentration,
pubmed-meshheading:3941108-Kinetics,
pubmed-meshheading:3941108-Liver,
pubmed-meshheading:3941108-Sonication,
pubmed-meshheading:3941108-Sulfhydryl Compounds
|
pubmed:year |
1986
|
pubmed:articleTitle |
Purification and properties of an (ADP-ribose)n glycohydrolase from guinea pig liver nuclei.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|