Linked Life Data

12126104

Source:http://linkedlifedata.com/resource/pubmed/id/12126104

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2002-7-19
pubmed:abstractText
Adenylate kinases modulate the three adenine nucleotide pools and were found to be localized as isoenzymes in different tissues and organelles in animals and plants. For investigations of adenylate kinase isoenzymes from plant tissues different plant extracts were examined by anion-exchange chromatography. During investigations with the strong anion exchanger Mono Q, adenylate kinase activity eluted in the void volume. This void volume activity did not always occur, but depended on the age of the plants and light treatment. The nature of the factors affecting void volume activity could only be partially resolved. It could be shown that RNase treatment at the beginning of extraction led to the disappearance of void volume activity, whereas an untreated extract still showed this activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9673
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
625
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13-9
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Adenylate kinase from plant tissues. Influence of ribonuclease on binding properties on Mono Q.
pubmed:affiliation
Institut für Biologie II, Universität Freiburg, Germany.
pubmed:publicationType
Journal Article