Linked Life Data

2635869

Source:http://linkedlifedata.com/resource/pubmed/id/2635869

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1990-6-18
pubmed:abstractText
(ADP-ribose)n glycohydrolase activity was inhibited in vitro by lignin, a naturally occurring polymethoxyphenolic compound. However, coniferyl alcohol, which is a main component of lignin, was not inhibitory even at 100 micrograms/ml. Lignin caused competitive inhibition with respect to the substrate (ADP-ribose)n and its Ki value was 18 micrograms/ml. These results suggest that lignin with a polymerized structure has a functional domain that interacts with the (ADP-ribose)n glycohydrolase molecule at the same site as (ADP-ribose)n.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0158-5231
pubmed:author
pubmed:issnType
Print
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1395-402
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Lignin inhibits (ADP-ribose)n glycohydrolase activity.
pubmed:affiliation
Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, Teikyo University, Kanagawa, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't