Purification and characterization from human parotid secretion of a peptide which inhibits hemagglutination of Bacteroides gingivalis 381.
A peptide from human parotid secretion which inhibited hemagglutination of Bacteroides gingivalis 381 was purified by ultrafiltration followed by DEAE-Sephadex A-25 column chromatography and by gel filtration on Sephadex G-25, and then by reversed-phase HPLC. The complete amino acid sequence of the peptide, determined by automated Edman degradation was as follows; Lys-Phe-His-Glu-Lys-His-His-Ser-His-Arg-Gly-Tyr. The peptide contained 12 residues and the charged amino acids predominated with 4 histidine, 2 lysine, 1 arginine and 1 glutamic acid residues, thus being a histidine-rich peptide. The peptide was an active inhibitor of the hemagglutinating activity of B. gingivalis. Specific binding of tritium-labeled peptide to B. gingivalis cells was demonstrated. These results suggest that the histidine-rich peptide may function as a binding domain for the hemagglutinins of B. gingivalis during agglutination.
Murakami
Y
Y
Department of Preventive Dentistry, Faculty of Dentistry, Osaka University, Japan.
Amano
A
A
Takagaki
M
M
Shizukuishi
S
S
Tsunemitsu
A
A
Aimoto
S
S
D000595:Amino Acid Sequence; D001439:Bacteroides / Q000378:metabolism*; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D006384:Hemagglutination / Q000187:drug effects*; D006385:Hemagglutination Inhibition Tests; D054808:Histatins; D006801:Humans; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000378:metabolism / Q000494:pharmacology*; D010306:Parotid Gland / Q000378:metabolism*; D014462:Ultrafiltration
C068075:HTN3 protein, human; D054808:Histatins; D009842:Oligopeptides