TY - JOUR
T1 - Biologically active polypeptides from the tropical sea anemone Radianthus macrodactylus
AU - Monastyrnaya, Margarita M.
AU - Zykova, Tatyana A.
AU - Apalikova, Olga V.
AU - Shwets, Tatyana V.
AU - Kozlovskaya, Emma P.
PY - 2002/1/1
Y1 - 2002/1/1
N2 - 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 1.0×104HU/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 20HU/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.
AB - 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 1.0×104HU/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 20HU/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.
KW - Actinoporins
KW - Cytolysins
KW - Hemolytic
KW - Histaminolytic activity
KW - Sphingomyelin
KW - Trypsin inhibitors
KW - Trypsin inhibitory activity
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U2 - 10.1016/S0041-0101(02)00139-3
DO - 10.1016/S0041-0101(02)00139-3
M3 - Article
C2 - 12165324
AN - SCOPUS:0035993555
SN - 0041-0101
VL - 40
SP - 1197
EP - 1217
JO - Toxicon
JF - Toxicon
IS - 8
ER -