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Flower development of Ranunculus asiaticus L. growing in the University Bo­tanic Garden was divided into six stages (I - VI): tight bud stage (I), loose bud stage (II), half open stage (III), open flower stage (IV), partially senescent stage (V) and senescent stage (VI). The average life span of an individual flower after it is fully open is about 5 days. Membrane permeability of sepal tissues estimated as electrical conductivity of ion leachates (^S), increased as the development proceeded through various stages. The content of sugars in the petal tissues increased during the flower opening period and then declined during senescence. The soluble proteins registered a consistent decrease with the simultaneous increase in specific protease activity and a-amino acid content during different stages of flower development and senescence. The content of total phenols registered an initial increase as the flowers opened, and then declined during senescence.
Proteases, also referred to as peptidases, are the enzymes that catalyse the hydrolysis of peptide bonds in polipeptides. A variety of biological functions and processes depend on their activity. Regardless of the organism’s complexity, peptidases are essential at every stage of life of every individual cell, since all protein molecules produced must be proteolytically processed and eventually recycled. Protease inhibitors play a crucial role in the required strict and multilevel control of the activity of proteases involved in processes conditioning both the physiological and pathophysiological functioning of an organism, as well as in host-pathogen interactions. This review describes the regulation of activity of bacterial proteases produced by dangerous human pathogens, focusing on the Staphylococcus genus.
The larvae of Anisakis simplex had the largest influence upon decreasing the activity of porcine pepsin. The activity of that enzyme in tests, where the larvae were present during the entire period of incubation, was lower than in the controls. No similar trends were observed in case of the solutions with bovine and porcine trypsin. The activity of those enzymes in the solutions containing the larvae was higher than in the controls. Only the activity of porcine trypsin after 10 h of incubation was slightly lower in the experimental sample than in the control, however, during the later hours the dynamics of the activity decrease of that enzyme in the controls was higher than in the experimental samples. The recorded activity of papain in the samples containing the larvae was higher than that in the controls during the entire time of the experiment.
The proteins level and activities of acid and alkaline proteases in whole body extracts of drone prepupae of Apis mellifera naturaly infested with Varroa destructor were studied. The infested and a non-infested group did not differ significantly in their total protein content. However, some differences in protein profiles were found. A lack of three protein fractions of moderate and lower molecular weight in infested prepupae was noted. Moreover, some differences in the quantity of protein in most of the fractions were observed. The activity of acid proteases from infested prepupae was lower (p < 0.05) compared with the activity of these proteases from the non-infested one group. The infested drone had higher activity of alkaline proteases than non-infested but this difference was not statisticaly significant.
Bacillus subtilis EAG-2 strain isolated from an ornamental plant nursery produced a highly active extracellular protease. It was purified to apparent homogeneity by successive purification steps. The SDS-gel of purified protease revealed a single band of 27 KDa on 10% polyacrylamide gel. Proteolytic activity was confirmed by using two different zymographic methods. Interestingly, the enzyme showed two clear activity bands in both cases. The optimum proteolysis for this protease was observed at pH 8.5 and 65°C. The enzyme was highly stable up to 80% after 30-50°C for 60 minutes. It also remained stable at pH 6.5-9.0 after 4 hours of incubation at 37°C. Its activity was reduced to 16% and 25% by PMSF and APMSF which indicates its relation to serine proteases. An increase in activity was noticed in the presence of Ca⁺², Zn⁺² and Ba⁺². On the other hand, it worked effectively with different natural substrates. Hence EAG-2 protease might be a useful contribution to the enzyme industry in Pakistan based upon its distinctive properties.
The study was conducted on a podzolic soil (originating from a field experiment), fertilized with various doses of municipal-industrial sewage sludge, i.e. 30 (1%), 75 (2.5%), 150 (5%), 300 (10%) and 600 Mg ha⁻¹ (20%), and then planted with willow (Salix viminalisL.). In the third year from setting up the experiment, in two layers of the soil (0-20 and 20-40 cm) determinations were made on the effect of the applied sludge on the respiratory activity, cellulose mineralization rate, intensification of ammonification and nitrification, and on dehydrogenases and protease activity. The results obtained showed a positive effect of the sludge on almost all of the analysed biochemical parameters, both in the surface and in the deeper layers of the soil. The effect of the sludge in the Ap horizon was more pronounced and generally increased with increasing dosage. Only the process of ammonification was subject to inhibition that was stronger in the surface horizon of the soil.
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