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Open AccessJournal ArticleDOI

Production and characterization of antibodies against microcystins.

TLDR
Indirect ELISA and RIA revealed that MCYST-LR-ethylenediamine-bovine serum albumin was a better immunogen and antibodies against a microcystin (MCYST) leucine-arginine variant were demonstrated 4 weeks after immunization of rabbits.
Abstract
Antibodies against a microcystin (MCYST) leucine-arginine variant (MCYST-LR) were demonstrated 4 weeks after immunization of rabbits with either MCYST-LR-polylysine- or MCYST-LR-ethylenediamine-modified bovine serum albumin. A radioimmunoassay (RIA), a direct competitive enzyme-linked immunosorbent assay (ELISA), and an indirect competitive ELISA were developed for characterization of the antibodies. Indirect ELISA and RIA revealed that MCYST-LR-ethylenediamine-bovine serum albumin was a better immunogen. Competitive RIA and direct ELISA revealed that the antibodies had good cross-reactivities with an MCYST-arginine-arginine variant (MCYST-RR), MCYST-LR, an MCYST-tyrosine-arginine variant (MCYST-YR), and nodularin (NODLN); but they had lower reactivities with variants MCYST-leucine-tyrosine (MCYST-LY) and MCYST-leucine-alanine (MCYST-LA). The antibodies did not cross-react with ozonolyzed MCYST-LR. The concentrations causing 50% inhibition of binding of reduced MCYST-LR to the antibodies by MCYST-RR, MCYST-LR, MCYST-YR, NODLN, MCYST-LA, and MCYST-LY in the RIA were 43, 105, 112, 503, 671, and 1,920 ng/ml, respectively. The concentrations causing 50% inhibition of binding of MCYST-LR-horseradish peroxidase to the antibodies by MCYST-RR, MCYST-LR, MCYST-YR, NODLN, MCYST-LY, and MCYST-LA in the ELISA were 1.75, 2.2, 3.4, 4.6, 50, and 114 ng/ml, respectively.

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Reference BookDOI

Toxic cyanobacteria in water: a guide to their public health consequences, monitoring and management.

TL;DR: The state of knowledge regarding the principal considerations in the design of programmes and studies for monitoring water resources and supplies and describes the approaches and procedures used as mentioned in this paper, and the information needed for protecting drinking water sources and recreational water bodies from the health hazards caused by cyanobacteria and their toxins.
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Effects of toxic cyanobacteria and purified toxins on the survival and feeding of a copepod and three species of Daphnia

TL;DR: The results suggest that zooplankton have evolved both physiological and behavioral adaptations which enhance their abilities to coexist with toxic cyanobacteria.
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Structure and biosynthesis of toxins from blue-green algae (cyanobacteria)

TL;DR: Nearly 30 new microcystins have been isolated in the laboratory from cyanobacteria species and their structures assigned, largely employing tandem FAB mass spectrometry (FABMS/CID/MS) and numerous analogs identified or synthesized allow the identification of important parameters in a structure-activity relationship study.
Journal ArticleDOI

Use of a colorimetric protein phosphatase inhibition assay and enzyme linked immunosorbent assay for the study of microcystins and nodularins

TL;DR: The results show the importance of Adda and glutamic acid in toxicity of these cyclic peptides and that PP1 inhibition is related to the toxins' mechanism of action.
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Journal ArticleDOI

The structure of cyanoginosin-LA, a cyclic heptapeptide toxin from the cyanobacterium Microcystis aeruginosa

TL;DR: The structure of cyanoginosin-LA (previously referred to by us as toxin BE-4) is cyclo(-D-Ala- L-Leu-erythro-β-methyl-D-isoAsp-L-AlA-Adda- D-Glu-N-methyldehydroAla) and a new nomenclature for the related toxins of Microcystis aeruginosa is discussed.
Journal ArticleDOI

Toxic peptides from freshwater cyanobacteria (blue-green algae). I. Isolation, purification and characterization of peptides from Microcystis aeruginosa and Anabaena flos-aquae.

TL;DR: Toxic peptides from two European Microcystis aeruginosa and one Canadian Anabaena flos-aquae species of freshwater cyanobacteria were purified by high performance liquid chromatography (HPLC) and examined by amino acid analysis and mass spectrometry.
Journal ArticleDOI

Analysis and purification of toxic peptides from cyanobacteria by reversed-phase high-performance liquid chromatography

TL;DR: A total system for the analysis and isolation of microcystins was established and the adsorptive powers of three commercially available C18 cartridges successfully applied to the clean up of three of the toxins.
Journal ArticleDOI

Toxicity and partial structure of a hepatotoxic peptide produced by the cyanobacterium Nodularia spumigena Mertens emend. L575 from New Zealand.

TL;DR: A clonal isolate of the filamentous brackish-water cyanobacterium Nodularia spumigena Mertens emend was found to produce a potent hepatotoxic peptide with chemical and toxicological properties similar to those of the hepatot toxic heptapeptides produced by other freshwater planktonic cyanobacteria.
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