Coelenterolysin: a hemolytic polypeptide associated with the coelenteric fluid of sea anemones

The gastrovascular fluids of the sea anemone Phymactis clematis display strong hemolytic activity, which has basic pH optimum, is thermolabile and is sensitive to proteases. The hemolytic agent from the gastrovascular fluid was partially purified by ammonium sulfate precipitation, chromatography on...

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Autores principales:	Meinardi, E., Azcurra, J.M., Florin-Christensen, M., Florin-Christensen, J.
Formato:	JOUR
Materias:	Coelenterolysin Gastrovascular fluid Phymactis clematis coelenterolysin sea anemone toxin unclassified drug article hemolysis nonhuman priority journal sea anemone Actiniaria Anemone Clematis
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_03050491_v109_n1_p153_Meinardi
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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spelling	todo:paper_03050491_v109_n1_p153_Meinardi2023-10-03T15:21:14Z Coelenterolysin: a hemolytic polypeptide associated with the coelenteric fluid of sea anemones Meinardi, E. Azcurra, J.M. Florin-Christensen, M. Florin-Christensen, J. Coelenterolysin Gastrovascular fluid Phymactis clematis coelenterolysin sea anemone toxin unclassified drug article hemolysis nonhuman priority journal sea anemone Actiniaria Anemone Clematis Phymactis clematis The gastrovascular fluids of the sea anemone Phymactis clematis display strong hemolytic activity, which has basic pH optimum, is thermolabile and is sensitive to proteases. The hemolytic agent from the gastrovascular fluid was partially purified by ammonium sulfate precipitation, chromatography on Dowex-50W cation exchanger and gel filtration on Sephadex G-50. A single peak elutes from the latter with an estimated mol. wt of 18,000. This elution pattern is unaffected if the chromatography is carried out in the presence of 5 M urea. These results indicate that the hemolytic activity is due to a single peptide or a group of peptides of similar size, which we here designate as "coelenterolysin". Coelenterolysin is also present in sea anemone tissue homogenates, is different from the nematocyst toxin and is not associated with phospholipase activities. It is inhibited by sphingomyelin. This is the first report of hemolytic polypeptides associated with the coelenteric fluid of sea anemones. Coelenterolysin may have a role in extracellular digestion, defense against predators and invasion of the coelenteron by foreign organisms. © 1994. Fil:Meinardi, E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Azcurra, J.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Florin-Christensen, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Florin-Christensen, J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_03050491_v109_n1_p153_Meinardi
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Coelenterolysin Gastrovascular fluid Phymactis clematis coelenterolysin sea anemone toxin unclassified drug article hemolysis nonhuman priority journal sea anemone Actiniaria Anemone Clematis Phymactis clematis
spellingShingle	Coelenterolysin Gastrovascular fluid Phymactis clematis coelenterolysin sea anemone toxin unclassified drug article hemolysis nonhuman priority journal sea anemone Actiniaria Anemone Clematis Phymactis clematis Meinardi, E. Azcurra, J.M. Florin-Christensen, M. Florin-Christensen, J. Coelenterolysin: a hemolytic polypeptide associated with the coelenteric fluid of sea anemones
topic_facet	Coelenterolysin Gastrovascular fluid Phymactis clematis coelenterolysin sea anemone toxin unclassified drug article hemolysis nonhuman priority journal sea anemone Actiniaria Anemone Clematis Phymactis clematis
description	The gastrovascular fluids of the sea anemone Phymactis clematis display strong hemolytic activity, which has basic pH optimum, is thermolabile and is sensitive to proteases. The hemolytic agent from the gastrovascular fluid was partially purified by ammonium sulfate precipitation, chromatography on Dowex-50W cation exchanger and gel filtration on Sephadex G-50. A single peak elutes from the latter with an estimated mol. wt of 18,000. This elution pattern is unaffected if the chromatography is carried out in the presence of 5 M urea. These results indicate that the hemolytic activity is due to a single peptide or a group of peptides of similar size, which we here designate as "coelenterolysin". Coelenterolysin is also present in sea anemone tissue homogenates, is different from the nematocyst toxin and is not associated with phospholipase activities. It is inhibited by sphingomyelin. This is the first report of hemolytic polypeptides associated with the coelenteric fluid of sea anemones. Coelenterolysin may have a role in extracellular digestion, defense against predators and invasion of the coelenteron by foreign organisms. © 1994.
format	JOUR
author	Meinardi, E. Azcurra, J.M. Florin-Christensen, M. Florin-Christensen, J.
author_facet	Meinardi, E. Azcurra, J.M. Florin-Christensen, M. Florin-Christensen, J.
author_sort	Meinardi, E.
title	Coelenterolysin: a hemolytic polypeptide associated with the coelenteric fluid of sea anemones
title_short	Coelenterolysin: a hemolytic polypeptide associated with the coelenteric fluid of sea anemones
title_full	Coelenterolysin: a hemolytic polypeptide associated with the coelenteric fluid of sea anemones
title_fullStr	Coelenterolysin: a hemolytic polypeptide associated with the coelenteric fluid of sea anemones
title_full_unstemmed	Coelenterolysin: a hemolytic polypeptide associated with the coelenteric fluid of sea anemones
title_sort	coelenterolysin: a hemolytic polypeptide associated with the coelenteric fluid of sea anemones
url	http://hdl.handle.net/20.500.12110/paper_03050491_v109_n1_p153_Meinardi
work_keys_str_mv	AT meinardie coelenterolysinahemolyticpolypeptideassociatedwiththecoelentericfluidofseaanemones AT azcurrajm coelenterolysinahemolyticpolypeptideassociatedwiththecoelentericfluidofseaanemones AT florinchristensenm coelenterolysinahemolyticpolypeptideassociatedwiththecoelentericfluidofseaanemones AT florinchristensenj coelenterolysinahemolyticpolypeptideassociatedwiththecoelentericfluidofseaanemones
_version_	1807315807410061312

Coelenterolysin: a hemolytic polypeptide associated with the coelenteric fluid of sea anemones

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