Linked Life Data

9176555

Source:http://linkedlifedata.com/resource/pubmed/id/9176555

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-6-20
pubmed:abstractText
Activity of nonspecific esterase from different tissues (i.e., liver, gallbladder, heart, intestine, and muscle) of five species of freshwater fish, namely, topmouth gudgeon (Pseudorasbora parva), goldfish (Carassius auratus), nile tilapia (Tilapia nilotica), mosquitofish (Gambusia affinis), and rainbow trout (Salmo gairdneri) was tested using alpha-naphthyl acetate as substrate. The results indicated that activity of the enzyme was mainly concentrated in the digestive system (i.e., intestine, liver, bile). The overall activity was highest in nile tilapia, followed by mosquitofish, topmouth gudgeon, goldfish, and lowest in rainbow trout. Electrophoresis and the following in vitro treatment of the isoenzymes with triphenol phosphate (TPP, an inhibitor of carboxylesterase) indicated the TPP-sensitive esterase was mainly distributed in liver of the five species. The enzyme was not found in the other five tissues (including gill) except in gallbladder of topmouth gudgeon and goldfish. The correlation was obviously improved between susceptibility and detoxification capacity if activity of the TPP-sensitive esterase was employed instead of that of the nonspecific esterase to make the comparison. In vitro treatment of nonspecific esterase in liver with malaoxon proved that the active metabolite of malathion inhibited a different isoenzyme from the TPP-sensitive one.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0098-4108
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
51
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
149-57
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Activity of esterases from different tissues of freshwater fish and responses of their isoenzymes to inhibitors.
pubmed:affiliation
Department of Plant Protection, Zhejiang Agricultural University, Hangzhou, Zhejiang Province, People's Republic of China.
pubmed:publicationType
Journal Article, In Vitro