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anemone hepatica/protease
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[Interaction investigation of trypsin inhibitor from sea anemone Radianthus macrodactylus with proteases].
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The interaction of inhibitor VJ (InhVJ), isolated from sea anemone R. macrodactylus, with different proteases was investigated. The following enzymes were tested: serine proteases (trypsin, alpha-chymotrypsin, plasmin, thrombin, kallikrein), cysteine protease (papain) and aspartic protease (pepsin).
Kunitz-type protease inhibitors from acrorhagi of three species of sea anemones.
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Sea anemones are rich in biologically active polypeptides such as toxins and protease inhibitors. These polypeptides have so far been isolated from whole bodies, tentacles or secreted mucus. Recently, two novel peptide toxins with crab lethality have been isolated from acrorhagi (specialized
Isolation and amino acid sequences of two Kunitz-type protease inhibitors from the sea anemone Anthopleura aff. xanthogrammica.
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Two protease inhibitors (AXPI-I and -II) were isolated from the sea anemone Anthopleura aff. xanthogrammica by a combination of acetone precipitation, gel filtration on Sephadex G-75, cation-exchange fast protein liquid chromatography (FPLC) on Mono S and reverse-phase HPLC on TSKgel ODS-120T. Both
[A serine protease inhibitor from the anemone Radianthus macrodactylus: isolation and physicochemical characteristics].
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A serine protease inhibitor with a molecular mass of 6106 +/- 2Da (designated as InhVJ) was isolated from the tropical anemone Radianthus macrodactylus by a combination of liquid chromatography methods. The molecule of InhVJ consists of 57 amino acid residues, has three disulfide bonds, and contains
A new multigene superfamily of Kunitz-type protease inhibitors from sea anemone Heteractis crispa.
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Despite a considerable number of publications devoted to isolation and physicochemical properties of protease inhibitors from sea anemones, virtually nothing is known about the structure of the genes, and the nature of their isoforms diversity. Using the PCR-based cloning approach we discovered the
A bifunctional sea anemone peptide with Kunitz type protease and potassium channel inhibiting properties.
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Sea anemone venom is a known source of interesting bioactive compounds, including peptide toxins which are invaluable tools for studying structure and function of voltage-gated potassium channels. APEKTx1 is a novel peptide isolated from the sea anemone Anthopleura elegantissima, containing 63 amino
Expression of sea anemone equistatin in potato. Effects of plant proteases on heterologous protein production.
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Plants are increasingly used as production platforms of various heterologous proteins, but rapid protein turnover can seriously limit the steady-state expression level. Little is known about specific plant proteases involved in this process. In an attempt to obtain potato (Solanum tuberosum cv
Two variants of the major serine protease inhibitor from the sea anemone Stichodactyla helianthus, expressed in Pichia pastoris.
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The major protease inhibitor from the sea anemone Stichodactyla helianthus (ShPI-1) is a non-specific inhibitor that binds trypsin and other trypsin-like enzymes, as well as chymotrypsin, and human neutrophil elastase. We performed site-directed mutagenesis of ShPI-1 to produce two variants
Equistatin, a protease inhibitor from the sea anemone actinia equina, is composed of three structural and functional domains.
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A cDNA encoding a precursor of equistatin, a potent cysteine and aspartic proteinase inhibitor, was isolated from the sea anemone Actinia equina. The deduced amino acid sequence of a 199-amino-acid residue mature protein with 20 cysteine residues, forming three structurally similar thyroglobulin
Chymotrypsin-like proteases from the sea anemone, Metridium senile.
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Amino acid analyses of chymotrypsin-like proteases from the sea anemone (Metridium senile).
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[Polyvalent protease inhibitors in sea anemones (Actinaria) with an inhibition spectrum analogous to that of the trypsin-kallikrein inhibitor from bovine organs].
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Hemolysins and proteinase inhibitors from sea anemones of the Gulf of Aqaba.
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Bioactive polypeptides have been isolated from three sea anemone species by gel filtration and ion-exchange chromatography: hemolysins from Gyrostoma helianthus and Radianthus koseirensis and proteinase inhibitors from the latter species and from Rhodactis rhodostoma. The hemolysins (molecular
Knockdown of actin and caspase gene expression by RNA interference in the symbiotic anemone Aiptasia pallida.
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Since the discovery of the ancient eukaryotic process of RNA-mediated gene silencing, the reverse-genetics technique RNA interference (RNAi) has increasingly been used to examine gene function in vertebrate and invertebrate systems. In this study, we report on the use of RNAi, adapted from studies
A simple biochemical method in the search for bioactive polypeptides in a sea anemone (Anemonia sulcata).
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The sea anemone Anemonia sulcata is a well-known natural source of supply of biologically active polypeptides. So far, five toxins, ATX I, II, III, IV and AS V, several polyvalent protease inhibitors, an elastase inhibitor, two blood pressure-depressive polypeptides and very recently peptides that
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