Abstrakt
The aim of the work was to determine the type and activity of body-surface proteases of bee workers kept in a natural habitat and in a cage. Samples were collected for five weeks.
40 cage samples and 50 hive samples were gathered, each containing 10 bees. Hydrophilic (watertreated) and hydrophobic (Triton-rinsed) proteins were isolated from the insects. The samples containing isolated proteins were tested as follows: protein concentration assay by the Lowry method; proteolytic activity in relation to various substrates (gelatine, haemoglobin, ovoalbumin, albumin, cytochrome C, casein) by the modified Anson method; proteolytic activity in relation to diagnostic inhibitors of proteolytic enzymes (pepstatin A, PMSF, iodoacetamide, o-phenantrolin), using the Lee & Lin method; acidic, neutral and basic protase activity by means of the modified Anson method; and electrophoretic analysis of proteins in a polyacrylamide gel for protease detection with the Laemmli method. The concentration of hydrophobic proteins on the body surface of the bees was found to be higher than that of hydrophilic proteins. Both in the hive and in the cage, proteolytic activity was observed only in relation to gelatine. The proteolytic activity of the hive bees remained at a steady level during the five weeks, whereas that of the cage bees varied. The hive workers were found to have aspartic, serine, thiolic and metallic proteases. On the other hand,
the cage bees had aspartic and serine proteases on their body surfaces.
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