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The mutual influence of proteins from Varroa destructor extracts and from honeybee haemolymph on their proteolytic activity – in vitro study

100%
Fraczek R. J., Zoltowska K., Lipinski Z., Dmitryjuk M.
Acta Parasitologica
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2013
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tom 58
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nr 3
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.
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Immunogenic potential of antigens isolated from trypsin pea protein hydrolysates

100%
Fraczek R. J., Kostyra E., Kostyra H.
Polish Journal of Food and Nutrition Sciences
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2008
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tom 58
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nr 4
The study was undertaken to examine the immunogenic potential of pea protein of Polish cultivar Maraton and its trypsin hydrolysates differing in a degree of hydrolysis. The physicochemical characteristics of a pea protein extract and its hydrolysates, DH 2.0 and 5.0, was conducted by means of SDS-PAGE electrophoresis, chromatofocusing, affinity chromatography, and sequential analysis. The immunogenic properties of pea protein and its trypsin hydrolysates, DH 2.0 and 5.0, were investigated by direct and competitive ELISA methods. The results confirm that the protein extract is a stronger immunogene than the hydrolysates, while hydrolysate with DH 2.0 was a stronger immunogene than that with DH 5.0. The dominant antigen isolated from the pea protein extract and both trypsin hydrolysates had a molecular weight of about 20 kDa and was in glycoprotein fraction. The N-terminal sequence of this antigen was determined to be: Thr-Glu-Thr-Thr-Ser-Phe-Leu-Ile-Thr-Lys. Its precursor is probably pea lectin.
3

Immunoreactive properties of pea protein extract and its trypsin hydrolysates

100%
Fraczek R. J., Kostyra E., Kostyra H., Krawczuk S.
Journal of Animal and Feed Sciences
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2007
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tom 16
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nr 3
472-484
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