Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1982-9-10
pubmed:abstractText
We have isolated an enzyme activity from extracts of Escherichia coli that catalyzes the hydrolysis of phosphodiester bonds in the single-stranded deoxyribopolymer (dU.[3H]dT)(2000) containing depyrimidinated sites created by enzymatic removal of uracil with uracil-DNA glycosylase. Nondepyrimidinated polymer is not degraded by the enzyme, nor is the depyrimidinated polymer degraded after reduction of apyrimidinic sites with sodium borohydride. The enzyme also degrades circular M13 DNA containing uracil or denatured phage PBS2 DNA (which naturally contains uracil) only after the removal of uracil from these substrates by uracil-DNA glycosylase. Undamaged or depurinated duplex PM2 or ColE1 DNA and undamaged M13 single-stranded DNA are not attacked by the enzyme. The activity sediments in glycerol gradients with a relative s value of 4.2 S and has a Stokes radius of 31 A, yielding a calculated Mr approximately 56,000. The fractional ratio (f/f0) is calculated at 1.25. The enzyme has no requirement for any known cofactors and is insensitive to inhibition by p-(chloromercuri)benzoate. Activity is inhibited in the presence of adenosine 5'0-triphosphate (ATP), tRNA or high ionic strength and is slightly stimulated by MnCl2 or CaCl2.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2548-56
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
An enzyme activity from Escherichia coli that attacks single-stranded deoxyribopolymers and single-stranded deoxyribonucleic acid containing apyrimidinic sites.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't