Statements in which the resource exists as a subject.
PredicateObject
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
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: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