Comparative amino acid sequence analysis of hemolysins produced by Vibrio hollisae and Vibrio parahaemolyticus.
Vibrio hollisae produces a hemolysin (Vh-rTDH) that is related to the thermostable direct hemolysin of Vibrio parahaemolyticus (Vp-TDH). Although both hemolysins are essentially similar biologically and immunologically, they differ markedly in heat stability; Vp-TDH is heat stable, whereas Vh-rTDH is heat labile. To elucidate the relationships between their characteristics and molecular structures, we analyzed the amino acid sequence of Vh-rTDH and compared it with that of Vp-TDH. Vh-rTDH consisted of 165 residues, of which 23 residues, spread over the peptide chain, differed from those of Vp-TDH.
Yoh
M
M
Department of Bacteriology and Serology, Osaka University, Japan.
Honda
T
T
Miwatani
T
T
Tsunasawa
S
S
Sakiyama
F
F
D000595:Amino Acid Sequence; D006460:Hemolysin Proteins / Q000235:genetics* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D012689:Sequence Homology, Nucleic Acid; D013045:Species Specificity; D013816:Thermodynamics; D014733:Vibrio / Q000235:genetics*
D006460:Hemolysin Proteins; D010446:Peptide Fragments