An endoproteolytic enzyme of Escherichia cd, designated protease III, has been purified about 9,600-fold to homogeneity with a 6% yield. The purified enzyme consists of a single polypeptide chain of M, 110,000 and is most active at pH 7.4. Protease III is very sensitive to metal-chelating agents and reducing agents. The EDTA-inactivated enzyme can be reactivated by Zn2+, Co’+ or Mn2+. Protease ...

The severe acute respiratory syndrome (SARS) coronavirus (CoV) main protease represents an attractive target for the development of novel anti-SARS agents. The tertiary structure of the protease consists of two distinct folds. One is the N-terminal chymotrypsin-like fold that consists of two structural domains and constitutes the catalytic machinery; the other is the C-terminal helical domain, ...

Protease producing bacteria was isolated from marine soil sample from Marakkanam Saltern, Tamil Nadu. Based on their morphology, it was identified as Pseudonomonas fluorescens biovar. The bacteria were inoculated in gelatin agar for the production of protease enzyme. The crude enzyme extract was purified by ammonium sulphate precipitation method to obtain 85% saturation. The protease enzyme act...

An intracellular protease was extracted and purified from Pseudomonas aeruginosa by ion-exchange chromatography on DEAE-cellulose followed by CM–cellulose and rechromatography on DEAE-cellulose. The purified protease was found to be homogeneous as judged by polyacrylamide disc gel electrophoresis (PAGE). The molecular mass of the protease as determined by gel filtration on G-150 was about 48,00...

Desquamation is described as a protease-dependent phenomenon where serine proteases with a basic pH optimum play a key role. Recently proteases with an acidic pH optimum were identified in the stratumcorneum and associated with desquamation, e.g., cathepsin D and the stratum corneum thiol protease. The purpose of this study was to investigate if human stratum corneum contains proteases differen...

A cysteine protease was characterized from Symbiodinium sp. strain KB8 isolated from Cassiopea ornata. The protease was purified 36-fold with a yield of 1.8%, by four chromatographic steps using DE-52, DEAE-Toyopearl, MonoQ, and Superdex 200 HR. Among the six substrates tested, the enzyme showed highest activity toward t-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumaryl-7-amide (Boc-VLK-MCA), and Z...

Structurally diverse organophosphonate inhibitors targeting the active site of the enzyme were used to investigate the relationship of the active site and the dimer interface of wild-type protease in solution. Positional scanning synthetic combinatorial libraries revealed Kaposi's sarcoma-associated herpesvirus protease to be highly specific, even at sites distal to the peptide bond undergoing ...

BACKGROUND The NS3 protease of hepatitis C virus (HCV) is a prime target for anti-HCV drugs but resistance towards inhibitors of the enzyme is likely to emerge because of mutations in the viral genome that modify the structure of the protein. Enzyme inhibition data supporting this is limited to studies with few compounds and analysis performed with truncated NS3. EXPERIMENTAL The potential of...

The thermoalkaline protease enzyme from pitaya (Hylocereus polyrhizus) waste was purified by a factor of 221.2 with 71.3% recovery using ammonium sulphate precipitation, gel filtration, and cation exchange chromatography. Gel filtration chromatography together with sodium dodecyl sulphate gel electrophoresis (SDS-PAGE) revealed that the enzyme is monomeric with a molecular weight of 26.7 kDa. T...

An extracellular protease was purified from Pseudomonas thermaerum GW1 a new strain identified by morphological, biochemical and 16S rDNA sequencing. It was isolated from soil of Poultry waste site at Ghazipur near Ghaziabad, Delhi. The strain produces extra cellular protease in the culture media that was maintained at 37°C, 140 rpm. The media was harvested for protease after 48 hrs of incubati...