| Literature DB >> 12183582 |
Takahiko Oho1, Morihide Mitoma, Toshihiko Koga.
Abstract
The bovine lactoferrin molecule and relatively long lactoferrin fragments containing residues 473 to 538 strongly inhibited adherence of Streptococcus mutans to saliva-coated hydroxyapatite beads. Each cysteine residue in Lf411 (residues 473 to 538) was replaced by a serine residue, and the mutants Lf411-C481S and Lf411-C532S strongly inhibited S. mutans adherence. These results suggest that the functional domain of lactoferrin that binds to a salivary film lies in residues 473 to 538 and that the region might be concealed by disulfide bond formation between Cys481 and Cys532 in the Lf411 fragment.Entities:
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Year: 2002 PMID: 12183582 PMCID: PMC128229 DOI: 10.1128/IAI.70.9.5279-5282.2002
Source DB: PubMed Journal: Infect Immun ISSN: 0019-9567 Impact factor: 3.441