Characterization of cholinesterase activity in larval Chironomus riparius meigen (= thummi kiefer)

1986 ◽  
Vol 16 (4) ◽  
pp. 733-739 ◽  
Author(s):  
Randall L. Detra ◽  
William J. Collins
Keyword(s):  
Cholinesterase Activity ◽  
Chironomus Riparius

Characterization of Hsp70 gene in Chironomus riparius: Expression in response to endocrine disrupting pollutants as a marker of ecotoxicological stress

2011 ◽  
Vol 153 (1) ◽  
pp. 150-158 ◽  
Author(s):  
Mónica Morales ◽  
Rosario Planelló ◽  
Pedro Martínez-Paz ◽  
Oscar Herrero ◽  
Estrella Cortés ◽  
...  
Keyword(s):  
Chironomus Riparius ◽  
Hsp70 Gene ◽  
Endocrine Disrupting

LOCALIZATION AND CHARACTERIZATION OF CHOLINESTERASE IN SUBCELLULAR FRACTIONS OF RAT BRAIN AND BEEF PITUITARY

1961 ◽  
Vol 39 (9) ◽  
pp. 1335-1345 ◽  
Author(s):  
Surendra S. Parmar ◽  
Morley C. Sutter ◽  
Mark Nickerson
Keyword(s):  
Rat Brain ◽  
Cholinesterase Activity ◽  
Succinic Dehydrogenase ◽  
Anterior Lobe ◽  
Subcellular Fractions ◽  
Posterior Pituitary ◽  
Low Concentrations ◽  
Pituitary Glands ◽  
Hydrolysis Of

Fresh rat brains and fresh anterior and posterior pituitary glands of beef were separated by differential centrifugation into subcellular fractions, characterized on the basis of sedimentation and succinic dehydrogenase activity. Cholinesterase activity was measured by both manometric and colorimetric methods, the results of which were comparable. Cholinesterase activity of rat brain was found mainly in the microsome and supernatant fractions. It was quite uniformly distributed in all subcellular fractions of both anterior and posterior pituitary. Comparisons of the relative rates of hydrolysis of acetylthiocholine and butyrylthiocholine, and of inhibition by eserine, indicated that brain contains a much higher percentage of acetylcholinesterase than do both lobes of the pituitary, which contain relatively low concentrations of the specific enzyme. Total cholinesterase activity and its sensitivity to inhibition by eserine in the posterior pituitary were found to be midway between those of the anterior lobe and of the brain, from which the posterior pituitary was derived during embryological development.

Characterization of cholinesterases in Chironomus riparius and the effects of three herbicides on chlorpyrifos toxicity

2013 ◽  
Vol 144-145 ◽  
pp. 296-302 ◽  
Author(s):  
Joanne Pérez ◽  
Marta S. Monteiro ◽  
Carla Quintaneiro ◽  
Amadeu M.V.M. Soares ◽  
Susana Loureiro
Keyword(s):  
Chironomus Riparius

Characterization of Lake Ladoga sediments. I. Toxicity to Chironomus riparius and Daphnia magna

Chemosphere ◽  
1996 ◽  
Vol 32 (6) ◽  
pp. 1165-1178 ◽  
Author(s):  
Tiina Ristola ◽  
Jukka Pellinen ◽  
Matti Leppänen ◽  
Jussi Kukkonen
Keyword(s):  
Daphnia Magna ◽  
Chironomus Riparius ◽  
Lake Ladoga

Characterization of Canine Hepatic and Renal Esterases

1973 ◽  
Vol 51 (5) ◽  
pp. 506-513 ◽  
Author(s):  
D. J. Ecobichon
Keyword(s):  
Cholinesterase Activity ◽  
Kinetic Characteristics ◽  
Migration Patterns ◽  
Tissue Extracts ◽  
Liver And Kidney ◽  
Inhibition Studies ◽  
Hydrolysis Of ◽  
Naphthyl Acetate ◽  
Substrate Hydrolysis

The esterases of canine liver and kidney were separated electrophoretically into nine bands with identical migration patterns in both tissues. An additional pair of rapidly migrating anodic bands were observed in hepatic extracts. Based on substrate specificity, the predominant tissue esterases were identified as nonspecific carboxylesterases (aliesterases). No cholinesterase activity was detected in the tissue extracts. Kinetic characteristics determined for the hepatic and renal esterases included (1) optimal pH; (2) Km values for esters of α-naphthyl and p-nitrophenol; (3) average rates of hydrolysis of α-naphthyl acetate and p-nitrophenyl acetate by the tissue extracts. Inhibition studies revealed the presence of two types of esterase activity in each tissue: one type being sensitive to organophosphorus esters, the second being resistant. A study of preferential substrate hydrolysis in the presence of known characteristic activators and inhibitors of esterases revealed approximately 5% and 20% arylesterase activity in liver and kidney, respectively. The presence of arylesterase activity in these tissues was confirmed by the hydrolysis of paraoxon (E600).

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