Search PubMed⌕ Search

Biomedical subjects

G Voss

Publications and source records attributed to G Voss.

At least 73 records · Page 4Linked to original sources
PubMed1979

Diethylmesoxalate hydrate, a new irreversible inhibitor of cholinesterases.

Bovine erythrocyte acetylcholinesterase and human plasma cholinesterase are irreversibly inhibited by diethylmesoxalate hydrate, the inhibition potency being comparable to that of certian insecticidal organophosphates and carbamates. Insect cholinesterases, however, appear to be much less affected by diethylmesoxalate hydrate. The compound was also found to inhibit the hydrolysis of paraoxon by rabbit plasma A-esterase, but in a reversible mode.

Animals↗
PubMed1977

MAO inhibition, an unlikely mode of action for chlordimeform.

Inhibition constants of several formamidines, their corresponding formanilides and other representatives of compounds derived from aniline, such as phenylureas, N-phenyl-carbamates and acylanilides, were determined for rat liver monoamine oxidase. The reversability of the inhibition and the lack of correlation between inhibition potencies and toxicities of the compounds tested add to the opinion that MAO inhibition is not a prominent factor in chlordimeform poisoning.

Amidines↗
PubMed1976

Some properties of cholinesterase of the plant nematode Aphelenchoides ritzema-boosi.

Activity and properties of cholinesterase from Aphelenchoides ritzema-boosi, a plant feeding nematode, were investigated by testing the reaction of the enzyme with different substrates and inhibitors. Butyrylthiocholine was a better substrate than propionyl- and acetylthiochine. When compared with mammaliian erythrocyte and plasma cholinesterase, the nematode enzyme was found to be extremely insensitive towards a number of well-known organophosphorus and carbamate inhibitors.

Acetylcholinesterase↗
PubMed1976

The effect of N-alkyl groups of substituted phenyl-N-alkyl carbamates on the inhibition of human plasma cholinesterase.

The inhibition constants for human plasma cholinesterase (dissociation, carbamylation, decarbamylation, overall bimolecular rate constants) were determined for two series of substituted phenyl-N-alkyl carbamates. N-propyl carbamates were found to be better inhibitors than the corresponding compounds carrying smaller N-alkyl groups. In both series the carbamylation constants of N-ethyl carbamates were lower than those of the N-methyl and N-propyl analogues, whereas the decarbamylation constants of the former were found to be higher than those of the latter carbamates. The experimental results obtained with human plasma cholinesterase are compared with published inhibition constants determined for several types of acetylcholinesterases.

Carbamates↗