Assuntos
Genes de Helmintos , Glicoproteínas/genética , Proteínas de Helminto/genética , Epitopos Imunodominantes/genética , Trichinella/genética , Animais , Sequência de Bases , Glicoproteínas/química , Glicoproteínas/imunologia , Proteínas de Helminto/química , Proteínas de Helminto/imunologia , Epitopos Imunodominantes/química , Camundongos , Dados de Sequência Molecular , Peso Molecular , Reação em Cadeia da Polimerase , Ratos , Trichinella/imunologiaRESUMO
A study was carried out on terminal, infiltrational and conductive anaesthetic activity of new aliphatic-aromatic aminoamides, C6H5CR(NHCOR'') - (CH2)nNR'2, which are the result of reaction between corresponding aminocarbinoles with nitriles in the presence of concentrated sulphuric acid. Terminal anaesthesia was checked on the rabbit eye cornea. Infiltrational anaesthesia was performed on guinea-pigs, conductive anaesthesia on frogs. A comparison of data on the local anaesthetic activity of aminoamides, aminoketones and aminoesters showed that aminoamides display a larger activity than aminoketones and are on the same scale as aminoesters. The choice of aminoamides made it possible to show the influence of various features of structure (lengths of hydrocarbon chain between functional groups, the nature of substitutes in the functional groups) on the local anaesthetic action of the preparations under study. It was proved that the increase of distance between the functional groups appreciably intensifies local anaesthetic activity. Moreover, substitution of the para and meta position by the benzene ring in the amide group leads to an increase of the anaesthetic effect.
Assuntos
Anestésicos Locais/farmacologia , Aminas/farmacologia , Anestésicos Locais/toxicidade , Animais , Cobaias , Técnicas In Vitro , Dose Letal Mediana , Camundongos , Coelhos , Relação Estrutura-AtividadeRESUMO
Butanol-1 and butandiol-1,4 are shown to increase the decarbamoylation rate of N-methylcarbamoyl- and N,N-dimethylcarbamoyl-cholinesterase. It is mainly due to the formation of a ternary complex NEA which is decomposed in 2,5 times faster than corbamoyl-enzyme EA. This is an evidence for the presence of some allosteric center in cholinesterase which is capable of binding alcohols.
Assuntos
Álcoois/farmacologia , Colinesterases/metabolismo , Sítio Alostérico , Butanóis/farmacologia , Butileno Glicóis/farmacologia , Química Orgânica , Fenômenos de Química OrgânicaRESUMO
It is shown that effect of alcohols ROH on the hydrolysis of butyryl-choline and acetylcholine by choline esterase (E. C. 3.1.1.8) is complex; it included the concurrent and the unconcurrent inhibitions, the interaction with the acylenzyme to form more reactive triple complex, and the acyl migration. By titrometric method it is found that proportion of the transacylation and hydrolysis rates depends on hydrophobity of R only being independent on its electronegativity.
