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The aim of the present study was to assess the haemolytic and proteolytic activity of coagulase- negative staphylococci (CNS) isolated from cows with mastitis. The study was conducted on 100 CNS strains: S. xylosus (n=28), S.chromogenes (n=26), S.haemolyticus (n=25), S. sciuri (n=14), S. warneri (n=4), S.hominis (n=2), S.saprophyticus (n=1); 22 CNS were isolated from cows with clinical mastitis and 78 from those with subclinical mastitis. The CNS studied showed the ability to produce only α-haemolysin and belonged to one strain – S. haemolyticus (21.0% of isolated CNS strains). Haemolysin-positive CNS were responsible for both clinical and subclinical mastitis (22.7% and 20.5%, respectively). The ability to produce protease was found in 31.0% of CNS belonging to two strains: S. chromogenes and S. sciuri. Protease-positive CNS were the etiological factor of both clinical and subclinical mastitis (31.8% and 30.8%, respectively). All S. xylosus, S. warneri, S. hominis, and S. saprophyticus strains were found protease-negative and haemolysin-negative, irrespective of whether they caused clinical or subclinical mastitis in cows.
 In the beginning of the 20th century, enzymes with proteolytic activity were classified as peptidases, Erepsin, and proteases. Among these, pepsin, trypsin, and autolytic enzymes were of the protease class. Spleen-derived proteases were poorly characterized until Sven Gustaf Hedin performed several digestion experiments with bovine spleen. He incubated minced bovine spleen under acidic or neutral conditions and characterized two active proteases; the results were published in 1903. The first protease was named α-protease and was active under neutral conditions. The second was named β-protease and was active under acidic conditions. We replicated Hedin's experiments according to his methods and found, by using activity-based probes to visualize proteases, that the historical α-protease is the present-day serine protease cathepsin G (CatG), which is known to be important in several immune processes, including antigen processing, chemotaxis, and activation of surface receptors. The β-protease, however, comprised different proteases including CatX, B, S, and D. We suggest that Hedin described CatG activity in bovine spleen over 100 years ago.
The influence of extracts from Varroa destructor, a parasitic mite of the honeybee Apis mellifera, on the proteinase activity of worker bee haemolymph was analysed in vitro, along with the influence of bee haemolymph on the proteolytic activity of V. destructor extract. The study was conducted in three different environments: pH 7.5 (high activity of bee enzymes and very low activity of parasite enzymes), pH 5 (moderate activity of enzymes from both sources) and pH 3.5 (limited activity of bee proteinases and high activity of mite proteinases). Based on electrophoretic studies, the inhibition of the activity of bee haemolymph proteinases by V. destructor extracts was observed at each pH. The study at pH 7.5 with commercial inhibitors of the 4 main classes of proteinases (pepstatin A, ethylenediaminetetraacetic acid (EDTA), E-64 (trans-epoxysuccinyl-L-leucylamido-(4-guanidino)-butane), soybean trypsin inhibitor and Kunitz inhibitor) suggested that parasite extracts mainly inhibited serine proteinases and, to a lower degree, cysteine and aspartyl proteinases. At pH 3.5 and pH 5, a decrease of approximately 40% in parasite proteinase activity was also observed in the presence of bee haemolymph. The result points to the presence of aspartyl proteinase inhibitors in bee haemolymph, which may be an important defence element for bees during food intake by a mite. It was demonstrated that trypsin and trypsin inhibitors are active in the excretion/secretion products of V. destructor, the proteinases of which may assist the parasite in food suckling by preventing haemolymph coagulation, among other things.
We carried out chymotryptic digestion of multimeric ATP-dependent Lon protease from Escherichia coli. Four regions sensitive to proteolytic digestion were located in the enzyme and several fragments corresponding to the individual structural domains of the enzyme or their combinations were isolated. It was shown that (i) unlike the known AAA+ proteins, the ATPase fragment (A) of Lon has no ATPase activity in spite of its ability to bind nucleotides, and it is monomeric in solution regardless of the presence of any effectors; (ii) the monomeric proteolytic domain (P) does not display proteolytic activity; (iii) in contrast to the inactive counterparts, the AP fragment is an oligomer and exhibits both the ATPase and proteolytic activities. However, unlike the full-length Lon, its AP fragment oligomerizes into a dimer or a tetramer only, exhibits the properties of a non-processive protease, and undergoes self-degradation upon ATP hydrolysis. These results reveal the crucial role played by the non-catalytic N fragment of Lon (including its coiled-coil region), as well as the contribution of individual domains to creation of the quaternary structure of the full-length enzyme, empowering its function as a processive protease
Leaf senescence allows plants to remobilise and use the same nitrogen repeatedly and is closely linked to autumn phenology. The timing of leaf senescence affects the growth rate and survival of trees due to the association between senescence and the remobilisation of nutrients, particularly nitrogen. The present study compares protein degradation dynamics and nitrogen remobilisation in early, intermediate and late phenological forms of beech trees (Fagus sylvatica L.). Specimens of phenological forms were marked and examined in 2005 and 2008. Leaf samples were collected from August to October during each of these years, and a biochemical analysis and a determination of proteolytic enzyme activity were conducted. The early phenological form showed protein degradation with three clearly indicated phases, whereas in the late form, protein degradation was stable with a constant decrease. The phenological forms differed significantly in their C/N ratios, which increased from approximately 20 in August to 37.5, 35 and 32 for the early, intermediate and late forms, respectively, at the end of leaf senescence. The date of the sudden drop in temperature had a decisive effect on the beginning of leaf senescence. Temperature has a greater effect on protein degradation and the protein and nitrogen resorption efficiency in the early form than in the late form. The trees that began to senesce the earliest exhibited the highest resorption of nitrogen compounds. Senescence led to an increase in proteolytic activity. Aminopeptidase activity was highest at the beginning of senescence, while endo- and carboxypeptidase activity was highest in the middle of senescence. The early form had the highest activity levels for all peptidase types. These results indicate that beech trees that differ in their autumn senescence timing display different nitrogen remobilisation efficiencies. This efficiency depended on the length of leaf senescence, peptidase activity and the sensitivity of particular phenological forms to temperature changes.
Investigations were conducted on the level of the overall proteolytic activity in flour fractions as well as fine and bruise bran, obtained from four varieties of wheat (‘Zyta’, ‘Pegassus’, ‘Sukces’, ‘Tonacja’), subjected to pre-harvest sprouting. Moreover, an analysis was conducted on the effect of pre-harvest sprouting on the functional properties of flour, determining the physical properties of gluten and dough. The analyses included a determination of crude protein, non-protein nitrogen, wet gluten, proteolytic activity and the rheologic properties of dough. The studies ended with a trial baking, with vitamin C and vital gluten added as improvers to the flour from pre-harvest sprouted grain. In all the milling fractions the overall proteolytic activity increased as result of sprouting, the highest increase being recorded for variety ‘Tonacja’. Simultaneously, in all the fractions tested an increased level of non-protein nitrogen was observed. Flour obtained from pre-harvest sprouted grain was characterised by an increased water holding capacity and the dough by poorer rheologic properties. Bread obtained from flour from pre-harvest sprouted grain was of insufficient quality. The use of improvers (vital gluten and vitamin C) as a rule resulted in favourable palatability and physico-chemical changes in bread
In the skin of diabetic animal tissues the amount of extracellular matrix (ECM) components is drastically decreased as a result of a reduced rate of their biosynthesis or increased degradation. In the present study we have investigated the mechanism of poor wound healing in diabetic rats. We have found that wounded skin of diabetic rats shows a significant decrease in glycosaminoglycan (GAG) content compared to that of control animals. This decrease was accompanied by significant depletion of insulin-like growth factor-I (IGF-I), known as a stimulator of GAG biosynthesis, and a distinct decrease in the content of high molecular weight IGF-binding proteins (HMW-BPs) with a simultaneous increase in low molecular weight IGF-binding proteins (LMW-BPs) in the sera of diabetic animals. Basing on determination of proteolytic activities we suggest that insulin shortage in diabetes results in increased proteolytic activity in various tissues. Proteolytic enzymes may cleave the HMW-BPs and convert them to LMW-BPs. The LMW-BPs may inactivate IGF-I and eliminate its stimulatory effects on GAG biosynthesis. The proteolytic enzymes may also digest the protein cores of proteoglycans releasing the GAGs and making them more susceptible to the action of glycosidases. These phenomena may be responsible for the observed marked decrease in GAG content in the skin of diabetic rats and disturb the wound-healing process.
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