Biomedical subjects

A Chaudhari

Publications and source records attributed to A Chaudhari.

50 records · Page 3Linked to original sources

PubMed1977

Correlation between antiinflammatory and antiproteolytic properties of substituted benzylidenes.

Twelve substituted benzylidenes were evaluated for antiinflammatory activity against carrageenin-induced edema in rats. The protection afforded by these compounds at a dose of 100 mg/kg, i.p., ranged from 30 to 60%. Sodium salicylate (100 mg/kg, i.p.), used as a reference drug, exhibited a 30% antiinflammatory activity under similar experimental conditions. The in vitro effects of substituted benzylidenes were also investigated on the activity of trypsin during hydrolysis of bovine serum albumin, serum glutamate oxaloacetate transaminase, serum glutamate pyruvate transaminase, and endogenous lipid peroxide formation by liver homogenates. These results have provided some correlation between antiinflammatory and antiproteolytic properties of substituted benzylidenes.

Animals↗

PubMed1976

Synthesis of N,N'-bis(3-substituted benzylideneaminopropyl)-piperazines and their anti-inflammatory, antiproteolytic, and anticonvulsant properties.

Some N,N'-bis(3-substituted benzylideneaminopropyl) piperazines were synthesized and characterized by their sharp melting points and elemental analyses. These substituted piperazines possessed anti-inflammatory activity, and the protection afforded by these compounds against carrageenan-induced edema ranged from 23 to 67%. The antiproteolytic activity of these piperazines was reflected by their ability to inhibit in vitro hydrolysis of bovine serum albumin and casein by trypsin. The inhibition of trypsin-induced hydrolysis was concentration dependent and competitive in nature.

Animals↗

PubMed1976

Antihemolytic and antiproteolytic properties of substituted thiosemicarbazidophenothiazines and thiazolidonylphenothiazines.

Antihemolytic and antiproteolytic properties of several 10-(1-acetyl-4-arylthiosemicarbazido) phenothiazines and their corresponding cyclized 10-(2-arylimino-3-acetylamino-4-thiazolidonyl) phenothiazines were investigated. In vitro protection of hypoosmotic hemolysis of human red blood cells by substituted thiosemicarbazidophenothiazines and substituted thiazolidonyl-phenothiazines was concentration dependent; the degree of protection ranged from 19 to 32 and 26 to 42%, respectively, at a final concentration of 0.1 mM. All phenothiazines exhibited antiproteolytic activity. The in vitro inhibition of trypsin-induced hydrolysis of bovine serum albumin by these phenothiazines was concentration dependent and competitive in nature; the degree of inhibition ranged from 30 to 50 and 32 to 79% for substituted thiosemicarbazidophenothiazines and substituted thiazolidonlyphenothiazines, respectively, at a concentration of 1mM. Cyclization of substituted thiosemicarbazidophenothiazines into the corresponding cyclized substitited thiazolidonlyphenothiazines increased the antihemolytic and antiproteolytic effectiveness of these phenothiazines.

Depression, Chemical↗

PubMed1976

Synthesis of substituted anilino-3-methoxy-4-substituted acetoxy) benzylidenes and their monoamine oxidase inhibitory and anticonvulsant properties.

Several substituted anilino-(3-methoxy-4-substituted acetoxy) benzylidenes were synthesized and characterized by their sharp melting points and elemental analyses. All substituted benzylidenes competitively inhibited the in vitro monoamine oxidase activity of rat brain homogenates and possessed anticonvulsant activity against pentylenetetrazol-induced convulsions in mice.

Animals↗

PubMed1976

Localization of oxalacetate keto-enol-tautomerase.

The intracellular location of oxalacetate keto-enol-tautomerase (oxaloacetate keto-enolisomerase) (EC 5.3.2.2) has been determined in two types of animal cells, rat liver and pig kidney. Two fractionation procedures were adopted and modified to suit each type of tissue. One fractionation procedure gave the soluble phase, microsomal and mitochondrial fractions, while the other isolated the nuclear fraction. The tautomerase is distributed among the soluble phase, microsomes and mitochondria in both tissues. Fractionation efficiency was checked by determining percentage recoveries of enzymic activity and total protein after each step, by microscopy studies and by determining the distribution of several marker enzymes.

Animals↗

PubMed1976