Purification and characterization of two hemolysins from Stichodactyla helianthus.
Two hemolysins, Sticholysin I (St I) and Sticholysin II (St II) were purified from the sea anemone Stichodactyla helianthus combining gel filtration and ion exchange chromatography. The amino acid composition of both cytolysins was determined revealing a high proportion of glycine, lysine, tyrosine and non-polar amino acids (alanine, leucine and valine). Cysteine was not found in either polypeptide. Molecular masses of St I and St II were 19401 and 19290 Da, respectively. N-terminal sequence analysis of St I and St II showed a high homology between them suggesting they are isoforms of the same cytolysin. Compared with other sea anemone cytolysins, St I and St II contain a 22 amino acid insertion fragment also present in Eq T II/Tn C and probably in CaT I and Hm T and absent in C III, the major hemolysin previously reported in this anemone.
Lanio
M E
ME
Department of Biochemistry, University of Havana, Cuba.
Morera
V
V
Alvarez
C
C
Tejuca
M
M
Gómez
T
T
Pazos
F
F
Besada
V
V
Martínez
D
D
Huerta
V
V
Padrón
G
G
de los Angeles Chávez
M
M
D000595:Amino Acid Sequence; D000818:Animals; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D003064:Cnidarian Venoms / Q000032:analysis / Q000302:isolation & purification*; D006460:Hemolysin Proteins / Q000032:analysis / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D009930:Organic Chemicals; D010455:Peptides / Q000032:analysis / Q000302:isolation & purification*; D012615:Sea Anemones
D003064:Cnidarian Venoms; D006460:Hemolysin Proteins; D009930:Organic Chemicals; D010455:Peptides; C404794:sticholysin II; C121348:stycholysin I