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Characterization of proteases in guts of Daphnia magna and their inhibition by Microcystis aeruginosa PCC 7806
10.1002/tox.20123.abs
Many cyanobacteria produce peptides that inhibit mammalian proteases. The hypothesis that inhibitors of mammalian proteases produced by cyanobacteria also interfere with digestive proteases of natural cladoceran grazers was tested by comparing the effects of cyanobacterial protease inhibitors on digestive proteases from Daphnia magna and on commercially available bovine proteases. The major digestive proteases of D. magna are trypsins and chymotrypsins, which differ from those of bovine origin in substrate specificity and susceptibility to synthetic inhibitors. An extract from Microcystis aeruginosa strain PCC 7806 inhibited both types of D. magna proteases. Subsequent fractionation of the extract by high‐performance liquid chromatography indicated that several inhibitors are produced by M. aeruginosa that differ in their specificity for the trypsins and chymotrypsins of D. magna. Two fractions differed in their inhibitory effect on proteases of D. magna and bovine origin; therefore, assessment of the impact of cyanobacterial protease inhibitors on natural communities requires the use of digestive proteases from ecologically relevant grazers. © 2005 Wiley Periodicals, Inc. Environ Toxicol 20: 314–322, 2005.
Characterization of proteases in guts of Daphnia magna and their inhibition by Microcystis aeruginosa PCC 7806
10.1002/tox.20123.abs
Many cyanobacteria produce peptides that inhibit mammalian proteases. The hypothesis that inhibitors of mammalian proteases produced by cyanobacteria also interfere with digestive proteases of natural cladoceran grazers was tested by comparing the effects of cyanobacterial protease inhibitors on digestive proteases from Daphnia magna and on commercially available bovine proteases. The major digestive proteases of D. magna are trypsins and chymotrypsins, which differ from those of bovine origin in substrate specificity and susceptibility to synthetic inhibitors. An extract from Microcystis aeruginosa strain PCC 7806 inhibited both types of D. magna proteases. Subsequent fractionation of the extract by high‐performance liquid chromatography indicated that several inhibitors are produced by M. aeruginosa that differ in their specificity for the trypsins and chymotrypsins of D. magna. Two fractions differed in their inhibitory effect on proteases of D. magna and bovine origin; therefore, assessment of the impact of cyanobacterial protease inhibitors on natural communities requires the use of digestive proteases from ecologically relevant grazers. © 2005 Wiley Periodicals, Inc. Environ Toxicol 20: 314–322, 2005.
Characterization of proteases in guts of Daphnia magna and their inhibition by Microcystis aeruginosa PCC 7806
Agrawal, Manish K. (Autor:in) / Zitt, Anja (Autor:in) / Bagchi, Divya (Autor:in) / Weckesser, Jürgen (Autor:in) / Bagchi, Suvendra N. (Autor:in) / von Elert, Eric (Autor:in)
Environmental Toxicology ; 20 ; 314-322
01.06.2005
9 pages
Aufsatz (Zeitschrift)
Elektronische Ressource
Englisch
protease , inhibitor , trypsin , peptide , chymotrypsin , microcystis , Daphnia , inhibition , cyanobacteria , microcystin
Contributions on Lindane Degradation by Microcystis aeruginosa PCC 7806
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