نتایج جستجو برای: proteinase activity

تعداد نتایج: 1142352  

Journal: :The Biochemical journal 1996
G Larcher B Cimon F Symoens G Tronchin D Chabasse J P Bouchara

An extracellular proteinase produced by the filamentous fungus Scedosporium apiospermum has been purified and characterized. Initially, in vitro conditions for enzyme synthesis were investigated. The highest yield of enzyme production was obtained when the fungus was cultivated in modified Czapek-Dox liquid medium supplemented with 0.1% bacteriological peptone and 1% (w/v) glucose as the nitrog...

Journal: :Infection and immunity 1989
M Padrines J G Bieth

Pseudomonas aeruginosa elastase rapidly inactivates alpha 1-proteinase inhibitor by splitting its Pro-357-Met-358 peptide bond. The present study was aimed at testing whether this reaction takes place in the presence of leukocyte elastase. To this end was added alpha 1-proteinase inhibitor to a mixture of the two elastases, and we performed the following assays: (i) measurement of the residual ...

Journal: :The Journal of clinical investigation 1993
S Reed J Bouvier A S Pollack J C Engel M Brown K Hirata X Que A Eakin P Hagblom F Gillin

Cysteine proteinases are hypothesized to be important virulence factors of Entamoeba histolytica, the causative agent of amebic dysentery and liver abscesses. The release of a histolytic cysteine proteinase from E. histolytica correlates with the pathogenicity of both axenic strains and recent clinical isolates as determined by clinical history of invasive disease, zymodeme analysis, and cytopa...

2016
Abhilash R. Jadhav Abdul R. War Ashwini N. Nikam Anmol S. Adhav Vidya S. Gupta Hari C. Sharma Ashok P. Giri Vaijayanti A. Tamhane

BACKGROUND Chilo partellus is an important insect pest infesting sorghum and maize. The larvae internalize in the stem, rendering difficulties in pest management. We investigated the effects of Capsicum annuum proteinase inhibitors (CanPIs) on C. partellus larvae by in-vitro and in-vivo experiments. METHODS Recombinant CanPI-7 (with four-Inhibitory Repeat Domains, IRDs), -22 (two-IRDs) and in...

Journal: :Journal of cell science 1987
E Krepela J Bártek D Skalková J Vicar D Rasnick J Taylor-Papadimitriou R C Hallowes

Human breast cancer cell lines, as well as transformed mammary epithelial cells (HBL-100) and growth-stimulated normal breast epithelial cells showed positive cytochemical reaction with the proteinase substrate 2-(N-benzyloxycarbonyl-L-arginyl-L-arginylamido)-4-methoxynapht halene, in the presence of 5-nitrosalicylaldehyde. The reaction product, small fluorescent granules, was distributed throu...

Journal: :The Journal of biological chemistry 1986
D L Mykles D M Skinner

Four Ca2+-dependent proteinase activities in lobster claw and abdominal muscle have been resolved by high-performance liquid chromatography on gel filtration and ion-exchange columns. These activities, which do not appear to be generated by autolytic or other degradative processes, differed from each other in molecular weight (peak I, Mr = 310,000; peak IIa, Mr = 125,000; peak IIb, Mr = 195,000...

2005
Guy S. SALVESEN Alan J. BARRETT

Although it is known that most of the plasma proteinase inhibitors form complexes with proteinases that are not dissociated by SDS (sodium dodecyl sulphate), there has been disagreement as to whether this is true for a2M ( a2-macroglobulin). We have examined the stability to SDS with reduction of complexes between a2M and several 125I-labelled proteinases (trypsin, plasmin, leucocyte elastase, ...

Journal: :The EMBO journal 1998
W R Lyon C M Gibson M G Caparon

The ability of numerous microorganisms to cause disease relies upon the highly regulated expression of secreted proteinases. In this study, mutagenesis with a novel derivative of Tn4001 was used to identify genes required for the expression of the secreted cysteine proteinase (SCP) of the pathogenic Gram-positive bacterium Streptococcus pyogenes. Designated as Rop loci (regulation of proteinase...

Journal: :The Journal of Experimental Medicine 1950
S. D. Elliott

Grown in dialysate broth at a pH between 5.5 and 6.5, some strains of group A streptococci elaborate the precursor of a proteolytic enzyme. Within this range of hydrogen concentration the precursor is also produced when the streptococci are suspended in a peptone dialysate containing glucose and incubated at 37 degrees C. The precursor does not appear to be produced at a neutral or alkaline rea...

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