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open-access-imgOpen AccessIsolation and some properties of exohemagglutinin from the culture medium of Bacteroides gingivalis 381
Author(s)
Eiji Inoshita,
Atsuo Amano,
Takashi Hanioka,
Hiroshi Tamagawa,
Satoshi Shizukuishi,
A. Tsunemitsu
Publication year1986
Publication title
infection and immunity
Resource typeJournals
PublisherAmerican Society for Microbiology
Exohemagglutinin was found in the culture medium of Bacteroides gingivalis 381. Exohemagglutinin was purified 3,150-fold from culture fluid by ultracentrifugation followed by gel filtration on Sepharose CL-4B and by affinity chromatography on arginine-agarose. Examination of the final preparation of exohemagglutinin by biochemical analysis and sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed that the isolated exohemagglutinin contained three major proteins but not a detectable lipopolysaccharide. Hemagglutination inhibition experiments showed that the activity of exohemagglutinin was inhibited by L-arginine and the arginine-containing peptides, although the activity was unaffected by the sugars tested. Some protein and glycoproteins that were examined also exhibited the inhibitory activity. When the bovine submaxillary mucin was chemically modified by beta-elimination and bovine serum albumin was modified by guanidination, the inhibitory effects on hemagglutination were significantly enhanced. These results suggest that the hemagglutination of the isolated exohemagglutinin may be involved in arginine residues as components of ligand-binding sites on erythrocytes.
Subject(s)affinity chromatography , amino acid , antibody , arginine , bacteria , bacteroidaceae , bacteroides , biochemistry , biology , bovine serum albumin , chemistry , chromatography , enzyme , gel electrophoresis , genetics , hemagglutination , hemagglutination assay , immunology , microbiology and biotechnology , mucin , polyacrylamide gel electrophoresis , titer
Language(s)English
SCImago Journal Rank1.508
H-Index220
eISSN1070-6313
pISSN0019-9567
DOI10.1128/iai.52.2.421-427.1986

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