Abstract:
: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.
journal_name
FEMS Microbiol Lettjournal_title
FEMS microbiology lettersauthors
Murakami Y,Amano A,Takagaki M,Shizukuishi S,Tsunemitsu A,Aimoto Sdoi
10.1016/0378-1097(90)90316-isubject
Has Abstractpub_date
1990-11-01 00:00:00pages
275-9issue
3eissn
0378-1097issn
1574-6968journal_volume
60pub_type
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