Biologically active polypeptides from the tropical sea anemone Radianthus macrodactylus. 2002

Margarita M Monastyrnaya, and Tatyana A Zykova, and Olga V Apalikova, and Tatyana V Shwets, and Emma P Kozlovskaya
Pacific Institute of Bioorganic Chemistry of the Far Eastern Branch of the Russian Academy of Sciences, pr. 100 let Vladivostoku 159, 690022, Vladivostok, Russian Federation. rita@piboc.dvo.ru

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 x 10(4), 5.0 x10(4), and 1.0 x10(4)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.

UI MeSH Term Description Entries
D007525 Isoelectric Focusing Electrophoresis in which a pH gradient is established in a gel medium and proteins migrate until they reach the site (or focus) at which the pH is equal to their isoelectric point. Electrofocusing,Focusing, Isoelectric
D007928 Lethal Dose 50 The dose amount of poisonous or toxic substance or dose of ionizing radiation required to kill 50% of the tested population. LD50,Dose 50, Lethal
D008055 Lipids A generic term for fats and lipoids, the alcohol-ether-soluble constituents of protoplasm, which are insoluble in water. They comprise the fats, fatty oils, essential oils, waxes, phospholipids, glycolipids, sulfolipids, aminolipids, chromolipids (lipochromes), and fatty acids. (Grant & Hackh's Chemical Dictionary, 5th ed) Lipid
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D010455 Peptides Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS. Peptide,Polypeptide,Polypeptides
D010741 Phospholipases A Phospholipases that hydrolyze one of the acyl groups of phosphoglycerides or glycerophosphatidates.
D011506 Proteins Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein. Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene
D002846 Chromatography, Affinity A chromatographic technique that utilizes the ability of biological molecules, often ANTIBODIES, to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Chromatography, Bioaffinity,Immunochromatography,Affinity Chromatography,Bioaffinity Chromatography
D002850 Chromatography, Gel Chromatography on non-ionic gels without regard to the mechanism of solute discrimination. Chromatography, Exclusion,Chromatography, Gel Permeation,Chromatography, Molecular Sieve,Gel Filtration,Gel Filtration Chromatography,Chromatography, Size Exclusion,Exclusion Chromatography,Gel Chromatography,Gel Permeation Chromatography,Molecular Sieve Chromatography,Chromatography, Gel Filtration,Exclusion Chromatography, Size,Filtration Chromatography, Gel,Filtration, Gel,Sieve Chromatography, Molecular,Size Exclusion Chromatography

Related Publications

Margarita M Monastyrnaya, and Tatyana A Zykova, and Olga V Apalikova, and Tatyana V Shwets, and Emma P Kozlovskaya
March 2007, Biochemistry. Biokhimiia,
Margarita M Monastyrnaya, and Tatyana A Zykova, and Olga V Apalikova, and Tatyana V Shwets, and Emma P Kozlovskaya
April 1979, Die Naturwissenschaften,
Margarita M Monastyrnaya, and Tatyana A Zykova, and Olga V Apalikova, and Tatyana V Shwets, and Emma P Kozlovskaya
November 1992, Toxicon : official journal of the International Society on Toxinology,
Margarita M Monastyrnaya, and Tatyana A Zykova, and Olga V Apalikova, and Tatyana V Shwets, and Emma P Kozlovskaya
May 1990, Bioorganicheskaia khimiia,
Margarita M Monastyrnaya, and Tatyana A Zykova, and Olga V Apalikova, and Tatyana V Shwets, and Emma P Kozlovskaya
July 1988, Bioorganicheskaia khimiia,
Margarita M Monastyrnaya, and Tatyana A Zykova, and Olga V Apalikova, and Tatyana V Shwets, and Emma P Kozlovskaya
January 1989, Toxicon : official journal of the International Society on Toxinology,
Margarita M Monastyrnaya, and Tatyana A Zykova, and Olga V Apalikova, and Tatyana V Shwets, and Emma P Kozlovskaya
January 2006, Biomeditsinskaia khimiia,
Margarita M Monastyrnaya, and Tatyana A Zykova, and Olga V Apalikova, and Tatyana V Shwets, and Emma P Kozlovskaya
January 1988, Doklady Akademii nauk SSSR,
Margarita M Monastyrnaya, and Tatyana A Zykova, and Olga V Apalikova, and Tatyana V Shwets, and Emma P Kozlovskaya
January 1984, Doklady Akademii nauk SSSR,
Margarita M Monastyrnaya, and Tatyana A Zykova, and Olga V Apalikova, and Tatyana V Shwets, and Emma P Kozlovskaya
January 1990, Toxicon : official journal of the International Society on Toxinology,
Copied contents to your clipboard!