THIOL-DEPENDENT SERINE PROTEINASES OF THERMOACTINOMYCES AND CERTAIN BACILLUS SPECIES - A NEW GROUP OF MICROBIAL PROTEOLYTIC ENZYMES

1985 ◽  
pp. 295-300
Author(s):  
V.M. Stepanov
Keyword(s):  
Proteolytic Enzymes ◽  
Bacillus Species ◽  
Serine Proteinases

scholarly journals Non-conventional affinity chromatography of serine proteinases and their inhibitors.

2003 ◽  
Vol 50 (3) ◽  
pp. 765-773 ◽  
Author(s):  
Antoni Polanowski ◽  
Anna Wilimowska-Pelc ◽  
Jolanta Kowalska ◽  
Joanna Grybel ◽  
Monika Zelazko ◽  
...  
Keyword(s):  
Affinity Chromatography ◽  
Proteinase Inhibitor ◽  
Proteolytic Enzymes ◽  
Trypsin Inhibitors ◽  
General Description ◽  
Separation Procedure ◽  
Serine Proteinases ◽  
High Concentration ◽  
Porcine Pancreas ◽  
Nacl Concentration

From among a wide variety of protein purification techniques affinity chromatography has proved to be particularly effective for separation of proteolytic enzymes and their inhibitors. In this article, following a general description of affinity adsorbents used for purification of proteinases, we overview a simple separation procedure for some serine proteinases and their inhibitors by way of affinity chromatography in the presence of high NaCl concentration. It has been shown that some highly specific trypsin inhibitors exhibit also antichymotrypsin activity when high concentration of Na(+) but not K(+) or Li(+) ions are present in the reaction mixture. Taking advantage of this phenomenon the virgin forms of trypsin inhibitors from squash seeds, Kazal-type inhibitor from porcine pancreas and alpha(1)-proteinase inhibitor from human and sheep plasma, as an example, were separated using immobilized chymotrypsin or its inactive derivative methylchymotrypsin in the presence of 5 M NaCl.

scholarly journals Complete Genome Sequence of the Mosquitocidal Bacterium Bacillus sphaericus C3-41 and Comparison with Those of Closely Related Bacillus Species

2008 ◽  
Vol 190 (8) ◽  
pp. 2892-2902 ◽  
Author(s):  
Xiaomin Hu ◽  
Wei Fan ◽  
Bei Han ◽  
Haizhou Liu ◽  
Dasheng Zheng ◽  
...  
Keyword(s):  
Genome Sequence ◽  
Complete Genome ◽  
Mosquito Control ◽  
Proteolytic Enzymes ◽  
Biological Control Agent ◽  
Sugar Transport ◽  
Bacillus Sphaericus ◽  
Transport Systems ◽  
Bacillus Species ◽  
Great Success

ABSTRACT Bacillus sphaericus strain C3-41 is an aerobic, mesophilic, spore-forming bacterium that has been used with great success in mosquito control programs worldwide. Genome sequencing revealed that the complete genome of this entomopathogenic bacterium is composed of a chromosomal replicon of 4,639,821 bp and a plasmid replicon of 177,642 bp, containing 4,786 and 186 potential protein-coding sequences, respectively. Comparison of the genome with other published sequences indicated that the B. sphaericus C3-41 chromosome is most similar to that of Bacillus sp. strain NRRL B-14905, a marine species that, like B. sphaericus, is unable to metabolize polysaccharides. The lack of key enzymes and sugar transport systems in the two bacteria appears to be the main reason for this inability, and the abundance of proteolytic enzymes and transport systems may endow these bacteria with exclusive metabolic pathways for a wide variety of organic compounds and amino acids. The genes shared between B. sphaericus C3-41 and Bacillus sp. strain NRRL B-14905, including mobile genetic elements, membrane-associated proteins, and transport systems, demonstrated that these two species are a biologically and phylogenetically divergent group. Knowledge of the genome sequence of B. sphaericus C3-41 thus increases our understanding of the bacilli and may also offer prospects for future genetic improvement of this important biological control agent.

scholarly journals Adsorption and inactivation of proteolytic enzymes by Triaenophorus nodulosus (Cestoda)

2017 ◽  
Vol 54 (1) ◽  
pp. 3-10 ◽  
Author(s):  
G.I. Izvekova ◽  
T.V. Frolova ◽  
E.I. Izvekov
Keyword(s):  
Proteolytic Activity ◽  
Incubation Medium ◽  
Proteolytic Enzymes ◽  
Surrounding Medium ◽  
Serine Proteinases ◽  
Suppressive Activity ◽  
Triaenophorus Nodulosus

Summary The proteolytic activity in washings off the Triaenophorus nodulosus cestode tegument and the ability of the worms to inactivate proteolytic enzymes were studied. It was found that the major proteolytic activity in the washing samples is represented by the easily desorbed fraction most probably characterizing the activity of the host’s enzymes. Serine proteinases are an essential part of these enzymes. It was shown that the worms’ incubation medium and their homogenates can inhibit host proteinases and commercial trypsin samples. Suppressive activity of the incubation medium suggests that the inhibitors are rather spontaneously produced by the worms than induced by the presence of proteinases in the surrounding medium. The inhibitor produced by the cestode is hypothesized to be trypsin-specific.

scholarly journals The effect of melanin on the proteolytic potential of blood under alkali esophageal burn

2020 ◽  
Vol 93 (1) ◽  
Author(s):  
Nataliia Chornenka ◽  
Liudmyla Domylivska ◽  
Olga Kravchenko ◽  
Tetiana Koval ◽  
Liza Torgalo ◽  
...  
Keyword(s):  
Proteolytic Activity ◽  
Proteinase Inhibitors ◽  
Proteolytic Enzymes ◽  
Biological Activities ◽  
Serine Proteinases ◽  
Medical Problems ◽  
Α2 Macroglobulin ◽  
Old Rats ◽  
Hydrolysis Of ◽  
Esophageal Burn

Caustic esophageal burns are among serious medical problems of global significance. Due to a key role in biological processes proteolytic enzymes actively involved in the pathological mechanisms underpinning the development and progression of burn-related complications. Since melanin possesses a broad spectrum of biological activities we have investigated whether this compound can influence the proteolytic activity and level of proteinase inhibitors in the blood of rats with an alkali esophageal burn. Alkaline esophageal burns, which correspond to the first and second degree of burn, were induced by 10% and 20% NaOH, respectively. White, nonlinear, immature (4 weeks old) rats were used in the experiment. Total proteolytic activity was measured using casein as a substrate. The activities of α1- antitrypsin and α2-macroglobulin were measured considering the degree of inhibition of hydrolysis of N-benzoyl-L-arginineethyl ester. The fraction of serine proteinases was obtained by affinity chromatography on a benzamidine sepharose column. The qualitative composition of serine proteinases fraction was analyzed by zymography technique. According to the data obtained, the pathogenesis of alkaline esophageal burn is accompanied by a significant increase in the total proteolytic activity, activity of serine proteinases, and activity of α1-antitrypsin and α2-macroglobulin compared with the control rats. The present results clearly indicated that melanin is able to normalize the proteolytic homeostasis by affecting the activity of serine proteinases and the level of proteinase inhibitors in the plasma of rats with alkali esophageal burns.

scholarly journals The presence and origin of phosphopeptides in human saliva

1988 ◽  
Vol 250 (1) ◽  
pp. 171-177 ◽  
Author(s):  
K Minaguchi ◽  
G Madapallimattam ◽  
A Bennick
Keyword(s):  
Oral Cavity ◽  
Calcium Binding ◽  
Proteolytic Enzymes ◽  
Biological Activities ◽  
Human Saliva ◽  
Serine Proteinases ◽  
Rapid Degradation ◽  
Whole Saliva ◽  
Oral Surface ◽  
Hydroxyapatite Formation

The presence of phosphopeptides in whole saliva (saliva expectorated from the mouth) was demonstrated and their origin was evaluated. Whole saliva contained much larger numbers of small phosphopeptides than are found in the glandular secretions. Most of these originated from the acidic proline-rich proteins (PRPs) in the major salivary glands and were formed, after secretion into the oral cavity, as a result of rapid degradation by proteolytic enzymes from extraglandular sources contained in sediment from whole saliva. Some peptides may have been formed by cleavage of basic PRPs, but other phosphoproteins apparently contributed little to the observed phosphopeptides. Most of the enzymes that produced phosphopeptides are serine proteinases. The gel-electrophoretic band patterns of the phosphopeptides obtained from 26 individuals of various acidic-PRP phenotypes were remarkably similar, demonstrating that the enzymes responsible were generally present in the population surveyed and that similar cleavages occur regardless of the nature of the acidic PRPs. Many of these peptides were N-terminal proteolytic cleavage products of acidic PRPs. The N-terminal phosphorylated region of acidic PRPs contains various biological activities, such as inhibition of hydroxyapatite formation, calcium binding and binding to hydroxyapatite, the major mineral of teeth. The demonstration of these phosphopeptides in the saliva that is in contact with the oral surface may therefore be of biological importance.

The ubiquitin–proteasome system and skeletal muscle wasting

2005 ◽  
Vol 41 ◽  
pp. 173-186 ◽  
Author(s):  
Didier Attaix ◽  
Sophie Ventadour ◽  
Audrey Codran ◽  
Daniel Béchet ◽  
Daniel Taillandier ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Wasting ◽  
Proteolytic Enzymes ◽  
Cathepsin L ◽  
Ubiquitin Proteasome System ◽  
Complete Breakdown ◽  
Skeletal Muscle Proteins ◽  
Ubiquitin Proteasome ◽  
Tripeptidyl Peptidase Ii ◽  
F Box Protein

The ubiquitin–proteasome system (UPS) is believed to degrade the major contractile skeletal muscle proteins and plays a major role in muscle wasting. Different and multiple events in the ubiquitination, deubiquitination and proteolytic machineries are responsible for the activation of the system and subsequent muscle wasting. However, other proteolytic enzymes act upstream (possibly m-calpain, cathepsin L, and/or caspase 3) and downstream (tripeptidyl-peptidase II and aminopeptidases) of the UPS, for the complete breakdown of the myofibrillar proteins into free amino acids. Recent studies have identified a few critical proteins that seem necessary for muscle wasting {i.e. the MAFbx (muscle atrophy F-box protein, also called atrogin-1) and MuRF-1 [muscle-specific RING (really interesting new gene) finger 1] ubiquitin–protein ligases}. The characterization of their signalling pathways is leading to new pharmacological approaches that can be useful to block or partially prevent muscle wasting in human patients.

Recent data on the causative agent of pale green dwarf (Acholeplasma laidlawii var. granulum incertae sedis) in Ukraine: pathogenicityand virulence factors and host reactions

2015 ◽  
Vol 2 (1) ◽  
pp. 30-34
Author(s):  
K. Korobkova ◽  
V. Patyka
Keyword(s):  
Phenylalanine Ammonia Lyase ◽  
Proteolytic Enzymes ◽  
Physiological State ◽  
Plant Cells ◽  
Temporary Increase ◽  
Adhesive Properties ◽  
The Impact ◽  
Signaling Interactions ◽  
Pale Green

Contemporary state of the distribution of mycoplasma diseases of cultivated crops in Ukraine was analyzed. The changes of the physiological state of plant cells under the impact of mollicutes were investigated. It was demonstrated that there is temporary increase in the activity of peroxidase, catalase, polyphenoloxidase, phenylalanine-ammonia-lyase at the early stages of interaction. The adhesive properties are changed in the mollicutes under the impact of plant lectin; there is synthesis of new polypeptides. It was determined that the phytopathogenic acholeplasma is capable of producing a complex of proteolytic enzymes into the culture me- dium. It was concluded that when plant cells are infected with acholeplasma, a number of signaling interactions and metabolic transformations condition the recognition of pathogenesis and ensure the aggregate response of a plant to stress in the form of defense reactions. It was assumed that some specifi cities of the biology of phy- topathogenic acholeplasma determine their avoiding the immune mechanisms of plants and promote long-term persistence of mollicutes.

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