Macrodactylus

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E P Kozlovskaya - One of the best experts on this subject based on the ideXlab platform.

  • study of the interaction of trypsin inhibitor from the sea anemone radianthus Macrodactylus with proteases
    Biochemistry (moscow) Supplement Series B: Biomedical Chemistry, 2007
    Co-Authors: I N Sokotun, O V Gnedenko, A A Molnar, M M Monastyrnaya, E P Kozlovskaya, A V Leychenko, A S Ivanov
    Abstract:

    The interaction of the inhibitor VJ (InhVJ), isolated from sea anemone R. Macrodactylus, with different proteases was investigated using the method of biosensor analysis. The following enzymes were tested: serine proteases (trypsin, α-chymotrypsin, plasmin, thrombin, kallikrein), cysteina protease (papain) and aspartic protease (pepsin). In the rage of the concentrations studied (10–400 nM) inhibitor VJ interacted only with trypsin and α-chymotrypsin. The intermolecular complexes formation between inhibitor VJ and each of these enzymes was characterized by the following kinetic and thermodynamics parameters: KD = 7.38 × 10−8 M and 9.93 × 10−7 M for pairs InhVJ/trypsin and InhVJ/α-chymotrypsin, respectively.

  • proteinase inhibitors from the tropical sea anemone radianthus Macrodactylus isolation and characteristic
    Biochemistry, 2007
    Co-Authors: I N Sokotun, Elena Leychenko, M M Monastyrnaya, A P Ilina, A A Eskov, S D Anastuk, E P Kozlovskaya
    Abstract:

    Two new serine proteinase inhibitors (RmIn I and RmIn II) from the tropical sea anemone Radianthus Macrodactylus have been isolated and characterized. The purification procedure includes polychrome-1 hydrophobic chromatography, Superdex™ Peptide 10/30 FPLC, and Nucleosil C18 reverse-phase HPLC. The molecular masses of RmIn I, RmIn II, and the complexes RmIn II/trypsin and RmIn I,II/α-chymotrypsin have been determined. The K i values of RmIn I and RmIn II for trypsin and α-chymotrypsin have been determined. The polypeptides RmIn I and RmIn II are shown to be nontoxic and to exhibit antihistamine activity. The N-terminal amino acid sequences of RmIn I (GICSEPIVVGPCKAG-) and RmIn II (GSTCLEPKVVGPCKA-) have been determined. A high homology of the amino acid sequences is demonstrated for the proteinase inhibitors produced by such evolutionarily distant species as coelenterates, reptiles, and mammals.

  • amino acid sequence of rtx a s isoform actinoporin from the sea anemone radianthus Macrodactylus
    Toxicon, 2006
    Co-Authors: Anna Ilina, A V Lipkin, Ekaterina V Barsova, Marina P Issaeva, Elena Leychenko, Konstantin V Guzev, M M Monastyrnaya, Sergey Lukyanov, E P Kozlovskaya
    Abstract:

    The amino acid sequence of actinoporin RTX-A (175 aa) from the sea anemone Radianthus Macrodactylus was determined by sequencing of clones obtained via amplification of cDNA. It was established that RTX-A possessed high homology with HmgIII from Heteractis magnifica (87%) and StI, StII from Stichodactyla helianthus (84 and 87%, respectively). The analysis of structural and functional relationships within RTX-A was carried out. The some disagreement concerning to significant role of several amino acid residues for actinoporins exhibition of hemolytic activity was found.

  • biologically active polypeptides from the tropical sea anemone radianthus Macrodactylus
    Toxicon, 2002
    Co-Authors: M M Monastyrnaya, Tatyana A Zykova, Olga V Apalikova, Tatyana V Shwets, E P Kozlovskaya
    Abstract:

    Abstract Some biologically active polypeptides, three high and two low molecular weight cytolysins and four trypsin inhibitors were isolated from the sea anemone Radianthus Macrodactylus and characterized. The purification steps involved acetone precipitation, gel filtration, ion-exchange, and affinity chromatography, and ion-exchange and reverse-phase HPLC. The relative molecular weight of high molecular weight Radianthus cytolysins named according to their N-terminal amino acids RTX-A (Ala), RTX-S (Ser) and RTX-G (Gly) was about 20,000. The isoelectric points were 9.8 for RTX-A and RTX-S, and 10.5 for RTX-G. The hemolytic activities of RTX-A, RTX-S and RTX-G were 3.5×104, 5.0×104, and 1.0×104 HU/mg, respectively, and were inhibited by sphingomyelin. The N-terminal amino acid sequence of RTX-A was determined as ALAGAIIAGAGLGLKILIEVLGEG–VKVKI–. Molecular weight of low molecular weight Radianthus cytolysins RmI, RmII, and of one trypsin inhibitor InI were 5100, 6100 and 7100, respectively. Isoelectric points for RmI and RmII were 9.2 and 9.3. Their hemolytic activity worked out 25 and 20 HU/mg, and was not inhibited by sphingomyelin. Toxicity of RmI and RmII was assessed by their histaminolytic activity. Amino acid composition of RmI and RmII was similar to that of tealiatoxin, histaminolytic cytolysin from the sea anemone Tealia felina.

  • sea anemone radianthus Macrodactylus a new source of palytoxin
    Toxicon, 1992
    Co-Authors: Vladimir M Mahnir, E P Kozlovskaya, Anatoly I Kalinovsky
    Abstract:

    A very potent non-protein toxin was isolated from the sea anemone Radianthus Macrodactylus with the use of chromatography on polytetrafluoroethylene, CM-Sephadex C-25 and by cation and anion exchange HPLC. The toxin was identified as palytoxin by u.v.-, i.r.- and 500 MHz 1H NMR spectroscopy. Its LD50 was 0.74 +/- 0.29 micrograms/kg by i.v. injection into mice. So far, palytoxin has been associated with zoanthids only. The toxin caused the loss of haemoglobin from erythrocytes but only in about 2 hr after the beginning of incubation, which is characteristic for palytoxin from zoanthids. Sea anemone palytoxin was divided into major and minor components by HPLC. The latter proved to be a product of degradation of palytoxin.

Miguel Ángel Morón - One of the best experts on this subject based on the ideXlab platform.

Roberto Arceperez - One of the best experts on this subject based on the ideXlab platform.

M M Monastyrnaya - One of the best experts on this subject based on the ideXlab platform.

  • study of the interaction of trypsin inhibitor from the sea anemone radianthus Macrodactylus with proteases
    Biochemistry (moscow) Supplement Series B: Biomedical Chemistry, 2007
    Co-Authors: I N Sokotun, O V Gnedenko, A A Molnar, M M Monastyrnaya, E P Kozlovskaya, A V Leychenko, A S Ivanov
    Abstract:

    The interaction of the inhibitor VJ (InhVJ), isolated from sea anemone R. Macrodactylus, with different proteases was investigated using the method of biosensor analysis. The following enzymes were tested: serine proteases (trypsin, α-chymotrypsin, plasmin, thrombin, kallikrein), cysteina protease (papain) and aspartic protease (pepsin). In the rage of the concentrations studied (10–400 nM) inhibitor VJ interacted only with trypsin and α-chymotrypsin. The intermolecular complexes formation between inhibitor VJ and each of these enzymes was characterized by the following kinetic and thermodynamics parameters: KD = 7.38 × 10−8 M and 9.93 × 10−7 M for pairs InhVJ/trypsin and InhVJ/α-chymotrypsin, respectively.

  • proteinase inhibitors from the tropical sea anemone radianthus Macrodactylus isolation and characteristic
    Biochemistry, 2007
    Co-Authors: I N Sokotun, Elena Leychenko, M M Monastyrnaya, A P Ilina, A A Eskov, S D Anastuk, E P Kozlovskaya
    Abstract:

    Two new serine proteinase inhibitors (RmIn I and RmIn II) from the tropical sea anemone Radianthus Macrodactylus have been isolated and characterized. The purification procedure includes polychrome-1 hydrophobic chromatography, Superdex™ Peptide 10/30 FPLC, and Nucleosil C18 reverse-phase HPLC. The molecular masses of RmIn I, RmIn II, and the complexes RmIn II/trypsin and RmIn I,II/α-chymotrypsin have been determined. The K i values of RmIn I and RmIn II for trypsin and α-chymotrypsin have been determined. The polypeptides RmIn I and RmIn II are shown to be nontoxic and to exhibit antihistamine activity. The N-terminal amino acid sequences of RmIn I (GICSEPIVVGPCKAG-) and RmIn II (GSTCLEPKVVGPCKA-) have been determined. A high homology of the amino acid sequences is demonstrated for the proteinase inhibitors produced by such evolutionarily distant species as coelenterates, reptiles, and mammals.

  • amino acid sequence of rtx a s isoform actinoporin from the sea anemone radianthus Macrodactylus
    Toxicon, 2006
    Co-Authors: Anna Ilina, A V Lipkin, Ekaterina V Barsova, Marina P Issaeva, Elena Leychenko, Konstantin V Guzev, M M Monastyrnaya, Sergey Lukyanov, E P Kozlovskaya
    Abstract:

    The amino acid sequence of actinoporin RTX-A (175 aa) from the sea anemone Radianthus Macrodactylus was determined by sequencing of clones obtained via amplification of cDNA. It was established that RTX-A possessed high homology with HmgIII from Heteractis magnifica (87%) and StI, StII from Stichodactyla helianthus (84 and 87%, respectively). The analysis of structural and functional relationships within RTX-A was carried out. The some disagreement concerning to significant role of several amino acid residues for actinoporins exhibition of hemolytic activity was found.

  • biologically active polypeptides from the tropical sea anemone radianthus Macrodactylus
    Toxicon, 2002
    Co-Authors: M M Monastyrnaya, Tatyana A Zykova, Olga V Apalikova, Tatyana V Shwets, E P Kozlovskaya
    Abstract:

    Abstract Some biologically active polypeptides, three high and two low molecular weight cytolysins and four trypsin inhibitors were isolated from the sea anemone Radianthus Macrodactylus and characterized. The purification steps involved acetone precipitation, gel filtration, ion-exchange, and affinity chromatography, and ion-exchange and reverse-phase HPLC. The relative molecular weight of high molecular weight Radianthus cytolysins named according to their N-terminal amino acids RTX-A (Ala), RTX-S (Ser) and RTX-G (Gly) was about 20,000. The isoelectric points were 9.8 for RTX-A and RTX-S, and 10.5 for RTX-G. The hemolytic activities of RTX-A, RTX-S and RTX-G were 3.5×104, 5.0×104, and 1.0×104 HU/mg, respectively, and were inhibited by sphingomyelin. The N-terminal amino acid sequence of RTX-A was determined as ALAGAIIAGAGLGLKILIEVLGEG–VKVKI–. Molecular weight of low molecular weight Radianthus cytolysins RmI, RmII, and of one trypsin inhibitor InI were 5100, 6100 and 7100, respectively. Isoelectric points for RmI and RmII were 9.2 and 9.3. Their hemolytic activity worked out 25 and 20 HU/mg, and was not inhibited by sphingomyelin. Toxicity of RmI and RmII was assessed by their histaminolytic activity. Amino acid composition of RmI and RmII was similar to that of tealiatoxin, histaminolytic cytolysin from the sea anemone Tealia felina.

  • calorimetric study of interactions of toxin from radianthus Macrodactylus with erythrocyte membrane
    Biochemistry international, 1992
    Co-Authors: V L Shnyrov, M M Monastyrnaya, G G Zhadan, S M Kuznetsova, E P Kozlovskaya
    Abstract:

    Differential scanning microcalorimetry, intrinsic protein fluorescence and SDS-electrophoresis have been applied for the study of the hemolytic toxin from sea anemone, Radianthus Macrodactylus, when it is incorporated into pure sphingomyelin/water systems and upon its effect on the human and dog erythrocyte membranes. The results obtained by using these techniques showed that one molecule of toxin withdraws six sphingomyelin molecules from the cooperative transition. Effect of hemolytic toxin on human erythrocyte ghosts causes an appearance of a new heat sorption peak in their differential scanning calorimetric curve with a maximum of 36 degrees C and, moreover, it leads to a loss of one of cytoskeleton proteins (actin). These effects are essentially weaker in the case of dog erythrocyte ghosts. This suggests differences in the structural organization of human and dog erythrocyte membranes.

Enrique Gonzalezortegon - One of the best experts on this subject based on the ideXlab platform.

  • assessment of the interaction between the white shrimp palaemon longirostris and the exotic oriental shrimp palaemon Macrodactylus in a european estuary sw spain
    Biological Invasions, 2010
    Co-Authors: Enrique Gonzalezortegon, Jose A Cuesta, E Pascual, Pilar Drake
    Abstract:

    Results of field surveys, stomach content analysis, and laboratory measurements of oxygen consumption at different salinities in the exotic shrimp Palaemon Macrodactylus and its native counterpart P. longirostris from the Guadalquivir estuary (SW Spain) were used to assess interaction between both species. After its first record in this estuary in 1998, P. Macrodactylus has shown a gradual increase in density and its estuarine population has been clearly dominated by juveniles. Feeding habits of both shrimps indicated a strong trophic overlap between them, with mysids as main prey. Their salinity-related and spatial distribution patterns show that maximal inter-specific overlap between the two populations occurs in the inner, less saline part of the estuary. Specific oxygen consumption rates under different salinities and water oxygen concentrations suggest a more efficient metabolism and a higher tolerance to hypoxic conditions in brackish waters by P. Macrodactylus than by P. longirostris. Such inter-specific physiological differences could have made it possible for the exotic P. Macrodactylus to invade an estuarine stretch that, prior to its arrival, was infra-utilized by native species.

  • first report of the oriental shrimp palaemon Macrodactylus rathbun 1902 decapoda caridea palaemonidae from german waters
    Helgoland Marine Research, 2007
    Co-Authors: Enrique Gonzalezortegon, Jose A Cuesta, Christoph D Schubart
    Abstract:

    The native East Asian shrimp Palaemon Macrodactylus has become a common inhabitant of estuaries along the Pacific coast of North America. More recently (documented since 1999), the species has also been colonising European waters and has been reported from Spain, England, Belgium and the Netherlands. In this study, we present a chronology of the reported introductions of this species and provide the first detailed report of its occurrence in German waters. P. Macrodactylus was found in the Geeste river mouth (Weser Estuary) as well as in Hooksiel, north of Wilhelmshaven between 2004 and 2005. We assume its presence in other estuarine habitats of the North Sea and predict its introduction into the Baltic Sea.

  • an illustrated key to species of palaemon and palaemonetes crustacea decapoda caridea from european waters including the alien species palaemon Macrodactylus
    Journal of the Marine Biological Association of the United Kingdom, 2006
    Co-Authors: Enrique Gonzalezortegon, Jose A Cuesta
    Abstract:

    A detailed illustrated key to the identi¢cation of the European species of the genera Palaemon and Palaemonetes is provided.This key has been elaborated taking into account recent changes in the species composition of both genera for European waters, such as the invalidity of Palaemon garciacidi, which is a synonym of P. longirostris, and the presence of an introduced species, Palaemon Macrodactylus that has been recently recorded at diierent localities along the Atlantic coast. The key is based on external morphological characters to facilitate its use by non-specialists. Data on the coloration, habitat and distribution of all species are also given.