Linked Life Data

9933965

Source:http://linkedlifedata.com/resource/pubmed/id/9933965

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11-12
pubmed:dateCreated
1999-2-26
pubmed:abstractText
The subcellular distribution of glutathione S-transferase (GST) activity extracted from shoots of 3-day-old etiolated seedlings of maize (Zea mays L., Northrup-King 9283 hybrid) and the induction of soluble and membrane-bound GST activity by the safener benoxacor, the herbicide metolachlor and their combination (CGA-180937) were investigated. GST activity extracted from maize shoots was detected in both cytosolic and microsomal fractions and utilized 1-chloro-2,4-dinitrobenzene (CDNB), metolachlor, and trans-cinnamic acid (CA) as substrates. Soluble GST activity extracted from maize shoots was greater than microsomal with CDNB or metolachlor as substrate. Membrane-bound GST activity was greater than soluble with cinnamic acid as substrate. Washing the microsomal preparations from maize shoots with Triton X-100 increased GST(CA) activity. Pretreatment with the safener benoxacor or a formulated combination of the herbicide metolachlor with benoxacor induced soluble GST(CDNB), GST(metolachlor) and GST(CA) activities in maize shoots. Benoxacor and CGA-180937 induced also membrane-bound GST(CDNB) and GST(CA) activities in maize shoots, but did not affect membrane-bound GST(metolachlor) activity. These results confirm that maize contains multiple GST isozymes that differ in their substrate specificity and inducibility by safeners or other chemicals.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0939-5075
pubmed:author
pubmed:issnType
Print
pubmed:volume
53
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
973-9
pubmed:dateRevised
2009-11-4
pubmed:meshHeading
pubmed:articleTitle
Influence of chemical treatments on glutathione S-transferases of maize with activity towards metolachlor and cinnamic acid.
pubmed:affiliation
Department of Biology, Frederick Community College, Maryland 21702, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't