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2012 | 68 | 10 |

Tytuł artykułu

Comparison of body-surface proteolytic activity of live and dead honey bee Apis mellifera workers

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
The aim of the study was to determine the type and activity of body-surface proteases of live and dead workers. Samples were collected for five weeks. 100 samples of live and dead worker bees were gathered, respectively, each containing 10 bees. The total number of samples was 200. Hydrophilic (water-treated) and hydrophobic (Triton-rinsed) proteins were isolated from the insects. The rinsing 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 a 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 protease 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 activity of aspartic and serine protease inhibitors by the Lee and Lin method; electrophoretic analysis of proteins in a polyacrylamide gel for protease inhibitor detection by means of a modified Felicioli method; and in vivo tests of antifungal and antibacterial activity using the double application method. The concentration of hydrophobic proteins on the body surface of the bees was found to be higher than that of hydrophilic proteins. The activity of proteases and their inhibitors remained at a steady level in the dead bees during the five weeks, whereas that of the live bees was variable. The dead workers were found to have aspartic, serine, thiolic and metallic proteases on the body surface; the live bees, in turn, had aspartic and serine proteases. The dead bees were less resistant to microorganisms. The methods used in the present study can be employed for assessing the condition and state of health of bee colonies, both prior to and after wintering, as well as during the beekeeping season.

Słowa kluczowe

Wydawca

-

Rocznik

Tom

68

Numer

10

Opis fizyczny

p.594-598,ref.

Twórcy

  • Department of Biological Basis of Animal Production, Faculty of Biology and Animal Breeding, University of Life Sciences in Lublin, Akademicka 13, 20-950 Lublin, Poland
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Bibliografia

  • 1.Anson M.: The estimation of pepsin, tripsin, papain and cathepsin with hemoglobin. J. Gen. Physiol. 1938, 22, 79-84.
  • 2.Barrett A. J.: Peptidases: a view of classification and nomenclature. Mol. Cell Biol. Updates 1999, 5, 1-12.
  • 3.Bertani G.: Studies on lysogenesis. I. The mode of phage liberation by lysogenic Escherichia coli. J. Bacteriol. 1952, 3, 293-300.
  • 4.Evans J. D., Aronstein K., Chen Y. P., Hetru C., Imler J. L., Jiang H., Kanost M., Thompson G. J., Zou Z., Hultmark D.: Immune pathways and defence mechanisms in honey bee Apis mellifera. Insect Mol. Biol. 2006, 15, 645-656.
  • 5.Felicioli R., Garzelli B., Vaccari L., Melfi D., Balestreri E.: Activity staining of protein inhibitors of proteases on gelatin-containing polyacrylamide gel electrophoresis. Anal. Biochem. 1997, 244, 176-179.
  • 6.Glisńki Z., Kostro K., Luft-Deptuła D.: Choroby pszczół. PWRiL, Warszawa 2006, 34-79.
  • 7.Grzywnowicz K., Ciołek A. (Strachecka), Tabor A., Jaszek M.: Profiles of body-surface proteolytic system of honey bee queens, workers and drones: Ontogenetic and seasonal changes in proteases and their natural inhibitors. Apidologie 2009, 40, 4-19.
  • 8.Laemmli U.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
  • 9.Lee T., Lin Y.: Trypsin inhibitor and trypsin-like protease activity in air - or submergence - grown rice (Oryza sativa L.) coleoptiles. Plant Sci. 1995, 106, 43-54.
  • 10.Murthy M., Rao B., Reddy N., Subrahmanyam P., Madhvanath U.: Non-equivalence of YEPD and synthetic complete media in yeast reversion studies. Mutat. Res. 1975, 2, 219-223.
  • 11.Paleolog J., Strachecka A., Burzyński S., Olszewski K., Borsuk G.: The larval diet supplemented with the low-molecular epigenetic switch sodium phenylacetylglutaminate influences the worker cuticle proteolytic system in Apis mellifera L. J. Apic. Sci. 2011, 55, 73-83.
  • 12.Sabouraud R.: Contribution a l'etude de la trichophytie humaine. Etude clinique, microscopique et bacterioloqique sur la pluralite des trichophytons de l'homme. Ann. Dermatol. Syphil. 1892, 3, 1061-1087.
  • 13.SAS Institute (2002-2003) SAS/STAT User's Guide release 9.13, Cary, NC, Statistical Analysis System Institute, license 86636.
  • 14.Schacterle G., Pollack R.: Simplified method for quantitative assay of small amounts of protein in biological material. Anal. Biochem. 1973, 51, 654-655.
  • 15.Strachecka A., Gryziñska M., Krauze M.: The influence of environmental pollution on the protective proteolytic barrier of the honey bee Apis mellifera mellifera. Polish J. Environ. Stud. 2010, 19, 855-859.
  • 16.Strachecka A., Paleolog J., Borsuk G., Gryzińska M., Olszewski K., Grzywnowicz K., Kasperek K.: Proteases on the body surface of honeybee Apis mellifera L. in cage and beehive. Annales Univ. Mariae Curie-Skłodowska 2011, 29, 106-112.
  • 17.Strachecka A., Paleolog J., Borsuk G., Olszewski K.: Influence of formic acid on the body surface proteolytic system at different developmental stages in Apis mellifera L. workers. J. Apic. Res. 2012, 51, 252-262.
  • 18.Strachecka A., Paleolog J., Borsuk G., Olszewski K., Grzywnowicz K., Gryzińska M.: Body-surface protease inhibitors in cage and hive Apis mellifera L. Acta Sci. Pol. 2011, 10, 125-132.
  • 19.Strachecka A., Paleolog J., Grzywnowicz K.: The surface proteolytic activity in Apis mellifera. J. Apic. Sci. 2008, 52, 49-56.

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