Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.1 (chymotrypsin)
 10,938 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Two distinct cytotoxic factors isolated from a Salmonella Gallinarum strain recovered from a bird died during an outbreak of fowl typhoid were purified to homogeneity through ciprofloxacin extraction, salt precipitation, dialysis, gelfiltration, ionexchange chromatography and chromatofocusing. These were designated as Salmonella Gallinarum cytotoxin I (GCT-I) and II (GCT-II). GCT-I was a glycoprotein having mol.wt and pI of Ca 70 kDa and 8.8, respectively. It was lethal to birds (LD50, 150 micrograms) inducing fowl typhoid like lesions. GCT-II, a protein with Ca 55 kDa mol.wt., was not lethal but caused haemorrhagic diarrhoea on intraperitoneal inoculation in birds. Both the cytotoxins induced cytopathic effects (CPE) in Vero and Madin Darby bovine kidney (MDBK) cells, enterotoxicity in rabbit ileal loop, dermatotoxicity in the rabbit skin and specific neutralizing antibodies in rabbits. These were active only between a narrow pH range of 6 to 8.5 and thermostable at 90 degrees C (1 min) but lost their activities on boiling. Trypsin and chymotrypsin enhanced their cytotoxicity, while pepsin, papain, protease, lipase and urea (5 M) had no appreciable effect on their cytotoxicity. Sodium carbonate (0.05 M) and formaldehyde (0.05%) had no effect on antigenicity of both the cytotoxic factors but rendered them nontoxic. Identification and characterization of cytotoxic moieties of S. Gallinarum not only reveals the important virulence factor but also indicates about the use of toxic factors as a candidate for toxoid vaccine and immunodiagnostics.
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PMID:Isolation and characterization of Salmonella Gallinarum cytotoxic factors. 1139 62

Stable polyelectrolyte microcapsules with size 6.5 microm were produced by means of the layer-by-layer adsorption of sodium alginate and protamine to surface of melamine formaldehyde microparticles. Core decomposition at low pH leads to formation of polyelectrolyte multilayered capsules filled with alginate gel. A proteolytic enzyme, alpha-chymotrypsin, was loaded into these microcapsules by embedding in alginate gel with high efficacy. The protein in the capsules was found to retain a high physiological activity of about 70% showed with fluorescent product. The protein was found to keep inside the microcapsules in water and acid (HCl solution, pH 1.7) during 24 and 4 h, respectively, while 75-85% of protein can be revealed in supernatant after 6 h incubation at pH 8.0 (0.05 M Tris buffer) in the presence of 2.5% w/v of sodium deoxycholate. The release rate of enzyme from multilayer alginate/protamine microcapsules can be regulated by additional adsorption of polyelectrolytes onto the microcapsules with encapsulated protein. Such protein-loaded capsules can be proposed as a drug delivery system with controllable release properties.
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PMID:Multilayer alginate/protamine microsized capsules: encapsulation of alpha-chymotrypsin and controlled release study. 1217 38

Chalcones and Mannich bases have been reported to present antiinflammatory activities as well as inhibitory activities on several factors implicated in inflammation disorders. A series of chalcones and some related Mannich bases were prepared by Claisen-Schmidt condensation of appropriate acetophenones with appropriate aromatic aldehyde. Mannich bases were derived from chalcones, with formaldehyde and the corresponding amine. The compounds were tested in vitro for their ability to inhibit various enzymes involved in the arachidonic acid cascade, for their antioxidant behaviour and in vivo for anti-inflammatory activity. Some chalcones and Mannich bases present strong anti-inflammatory and antioxidant activities. Almost all the tested compounds present high inhibitory activity on lipid peroxidation. Some compounds showed potent inhibitory effect on superoxide anion formation. Among the tested compounds 5 and 6 showed the highest lipoxygenase (LO) inhibitory activity. All the tested compounds inhibit both the proteolytic and esteratic activities of trypsin and chymotrypsin. The results indicated that the anti-inflammatory effects of the compounds were partially mediated, through their antioxidant activity. Attempts to correlate quantitatively structure with activity revealed that lipophilicity and molar refractivity influence the biological response.
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PMID:Synthesis and anti-inflammatory activity of chalcones and related Mannich bases. 1899 44

Spherical carbon aerogels (SCAs) with controlled particle size and mesopore size were synthesized by an emulsified sol-gel polymerization of phenol, melamine and formaldehyde. The adsorption rate and capacity of biomolecules with different molecular dimensions, including L-phenylalanine (Phe), vitamin B(12) (VB), alpha-chymotrypsin (Chy) and bovine serum albumin (BSA) onto SCAs were investigated. The mesopore size can be easily tuned in the range from 5 to 10 nm by simply adjusting catalyst concentration in the initial solution and the spherical particle size can be controlled in 50-500 microm by changing stirring speed. The as-prepared SCAs have high specific surface area (>600 m(2)/g) and large pore volume (>1 cm(3)/g). The hardness of SCAs is ca. 10 times as large as that of commercial spherical activated carbon particles. The adsorption rate of VB is strongly depended on the mesopore size and particle size, and show an increasing tread with the increase of mesopore size and the decrease of particle size. For small molecule Phe, the specific surface area is key factor to determine the adsorption capacity, but the adsorption capacity of large molecules (VB, Chy and BSA) is dependent on the pore size of SCAs, which should be suitably larger than the molecule size of biomolecules.
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PMID:Biomolecular adsorption behavior on spherical carbon aerogels with various mesopore sizes. 1906 32


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