Linked Life Data

8250911

Source:http://linkedlifedata.com/resource/pubmed/id/8250911

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1994-1-4
pubmed:abstractText
Renaturation gel assays are good tools to assign enzymatic activities to protein bands. First, proteins are separated by denaturating electrophoresis on substrate-containing gels. Then, following the elimination of the denaturing agent, polypeptides are allowed to renature, thus leading to the degradation of the embedded substrate at positions at which the corresponding activity has moved. Nevertheless, this in situ technique does not only reflect a certain amount of enzyme activity, it also depends upon the ability of an enzyme to renature. Here we present a renaturation gel assay procedure with an improved sensitivity and discuss the detection of E. coli and human ribonuclease H activities as an example.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
196
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1552-7
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Sensitive detection of low levels of ribonuclease H activity by an improved renaturation gel assay.
pubmed:affiliation
Laboratoire de Biophysique Moléculaire, INSERM CJF 90-13, Université de Bordeaux II, France.
pubmed:publicationType
Journal Article