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Comparison of the characteristics of a hydrophilic variant of Streptococcus gordonii ATCC 10558 and a hydrophilic variant of Streptococcus mutans Ingbritt

Arihide Kamaguchi, Hisae Baba

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Abstract

We isolated the hydrophilic variant of Streptococcus gordonn ATCC 10558 by the isolation procedure for the hydrophilic variant of Streptococcus mutans Ingbntt. The hydrophobicity of the variant of 5 S gordonn ATCC 10558 was lower than that of the parent strain, but adherence to salivary coated hydroxyapatite (S-HA) was not lower. The hydrophilic variant of 5 gordonn ATCC 10558 released more quantity of proteins of various molecular weights into the culture supernatant than parent strain. The findings suggest that the adhesin of S. gordonii ATCC 10558 to S-HA differs from the components causing cell surface hydrophobicity in S mutans Ingbntt.

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What this paper is about

We isolated the hydrophilic variant of Streptococcus gordonn ATCC 10558 by the isolation procedure for the hydrophilic variant of Streptococcus mutans Ingbntt. The hydrophobicity of the variant of 5 S gordonn ATCC 10558 was lower than that of the parent strain, but adherence to salivary coated hydroxyapatite (S-HA) was not lower. The hydrophilic variant of 5 gordonn ATCC 10558 released more quantity of proteins of various molecular weights into the culture supernatant than parent strain. The findings suggest that the adhesin of S. gordonii ATCC 10558 to S-HA differs from the components causing cell surface hydrophobicity in S mutans Ingbntt.

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Available abstract

We isolated the hydrophilic variant of Streptococcus gordonn ATCC 10558 by the isolation procedure for the hydrophilic variant of Streptococcus mutans Ingbntt. The hydrophobicity of the variant of 5 S gordonn ATCC 10558 was lower than that of the parent strain, but adherence to salivary coated hydroxyapatite (S-HA) was not lower. The hydrophilic variant of 5 gordonn ATCC 10558 released more quantity of proteins of various molecular weights into the culture supernatant than parent strain. The findings suggest that the adhesin of S. gordonii ATCC 10558 to S-HA differs from the components causing cell surface hydrophobicity in S mutans Ingbntt.

Key concepts: Streptococcus gordonii, Streptococcus mutans, Microbiology, Streptococcus, Chemistry, Streptococcaceae, Streptococcus sanguinis, Biology

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Comparison of the characteristics of a hydrophilic variant of Streptococcus gordonii ATCC 10558 and a hydrophilic variant of Streptococcus mutans Ingbritt — Research Paper | ScholarLens