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H Kuramitsu

Publications and source records attributed to H Kuramitsu.

At least 37 records · Page 2Linked to original sources
PubMed1990

Conservation of the regulatory subunit for the Clp ATP-dependent protease in prokaryotes and eukaryotes.

Bacteria, tomatoes, and trypanosomes all contain genes for a large protein with extensive homology to the regulatory subunit, ClpA, of the ATP-dependent protease of Escherichia coli, Clp. All members of the family have between 756 and 926 amino acids and contain two large regions, of 233 and 192 amino acids, each containing consensus sequences for nucleotide binding. Within these regions there is at least 85% similarity between the most distant members of the family. The high degree of similarity among the ClpA-like proteins suggests that Clp-like proteases are likely to be important participants in energy-dependent proteolysis in prokaryotic and eukaryotic cells.

ATP-Dependent Proteases↗
PubMed1983

Chemical characterization of extracellular polysaccharides produced by Actinomyces viscosus T14V and T14Av.

The human isolates Actinomyces viscosus T14V and T14Av produced extracellular polysaccharides in the absence of sucrose. In contrast to strain T14V, strain T14Av produced abundant viscous slime polysaccharide in the culture supernatant fluids when grown in a chemically defined medium containing glucose. After resolution of the T14Av polysaccharides into seven fractions, it was demonstrated that two of these exhibited viscous properties and lacked methylpentose and muramic acid. The major slime polysaccharide purified by gel filtration and ion-exchange column chromatography contained 39% (moles percent carbohydrate) galactose, 37% N-acetylglucosamine, 19% glucose, and 5% mannose. Only trace amounts of protein and phosphorus were detected in this preparation. On the other hand, strain T14V produced negligible slime polysaccharide under the same culture conditions. The major extracellular polysaccharide fraction from this strain contained methylpentoses, hexoses, hexosamines, muramic acid, protein, and phosphorus, suggesting that this fraction might be derived from the cell wall.

Actinomyces↗
PubMed1977

Molecular basis for the different sucrose-dependent adherence properties of Streptococcus mutans and Streptococcus sanguis.

The enzymatic and adherence properties of Streptococcus mutans GS5 and S. sanguis ST3, both isolated from human carious lesions, have been compared. During growth in sucrose media, S. mutans GS5 adheres to smooth surfaces approximately three times more effectively than dose S. sanguis ST3. However, strain ST3 does not display sucrose-dependent adherence under nongrowth conditions, whereas strain GS5 displays significant adherence. Although both organisms synthesize both water-soluble and -insoluble glucans, the glucosyltransferases from S. mutans GS5 synthesize much more adherent glucan molecules than do the comparable enzymes from S. sanguis ST3. Both cell types bind exogenous glucosyltransferases synthesized by strain ST3 equally well, whereas cells of strain GS5 bind the comparable enzyme fraction that it synthesizes to a greater degree than do cell of S. sanguis ST3. However, in contrast to the results with cells of S. mutans GS5, the absorption of the glucosyltransferase activity synthesized by S. mutans GS5 to the surface of S. sanguis ST3 results in low levels of subsequent sucrose-dependent adherence. These results are discussed in terms of the molecular basis for the sucrose-dependent adherence of the oral streptococci to smooth surfaces.

Adhesiveness↗
PubMed1976

Immunological relationships between glucosyltransferases from Streptococcus mutans serotypes.

Partially purified glycosyltransferase enzymes for Streptococcus mutans GS-5 (serotype c) have been utilized to prepare antibodies directed against the soluble glucan-synthesizing activity, GTF-B, and the insoluble-soluble glucan synthetic activity, GTF-A. Anti-GTF-A inhibited insoluble glucan formation catalyzed by the extracellular enzymes from strains GS-5 and FA-1 (serotype b) to a much greater extent than that of strains HS-6 (serotype a) or OMZ-176 (serotype d). This antibody fraction also inhibited both the cell-associated glucosyltransferase activities as well as the sucrose-mediated adherence of cells to glass surfaces by strains GS-5 and FA-1 but not that of strains HS-6 and OMZ-176. Anti-GTF-B inhibited soluble glucan formation catalyzed by the extracellular enzymes of strains GS-5 but not that of strain HS-6, FA-1, or OMZ-176. However, this antibody fraction did not strongly inhibit either the cell-associated glycosyltransferase activity or cellular adherence of any of the four strains. These results with body antibody fractions were also correlated with the ability of the antibodies to agglutinate the cells and form precipitin bands after immunodiffusion with the extracellular enzymes. Antibody prepared against the homogeneous soluble glucan-synthesizing enzyme demonstrated similar effects to the anti-GTF-B fraction. These results are discussed in terms of the antigenic relationships existing between the glucosyltransferases from different serotypes of S. mutans.

Antibodies, Bacterial↗