PubMed Health⌕ Search

Biomedical subjects

S Ono

Publications and source records attributed to S Ono.

At least 829 records · Page 46Linked to original sources
PubMed1979

Prophylactic effect of BCG cell-wall skeleton on the tumor induction by 7,12-dimethylbenz[a]anthracene in mice: strain difference.

Prophylactic effect of repeated intravenous administrations of oil-attached BCG cell-wall skeleton (BCG-CWS) on the induction of tumor by 7,12-dimethylbenz[a]anthracene (DMBA) was investigated in various strains of mice. The subcutaneous injection of DMBA emulsified in oil induced squamous cell carcinoma in almost all of the strains of mice. Treatment of C57BL/6, BALB/c, and ddO strains with BCG-CWS with appropriate route and timing resulted in the retardation of DMBA-induced tumor development manifested by a prolonged latent period of tumor outgrowth. In contrast, the same BCG-CWS treatment of C3H/He and BTK mice was incapable in preventing such DMBA-induced carcinogenesis. Thus, the treatment with BCG-CWS was effective for preventing the DMBA-induced carcinogenesis in certain strains of mice, but the effectiveness varied depending on the strain. The implication of such a strain variationof the BCG-CWS effect on the prophylaxis of chemical carcinogenesis was discussed in the context of differences in the magnitude of immunopotentiation of the host by BCG-CWS.

9,10-Dimethyl-1,2-benzanthracene↗
PubMed1979

Induction of the FAD synthetase system in rat liver by phenobarbital administration.

FMN and FAD synthesizing activities in rat liver were investigated when drug metabolizing enzymes were induced by phenobarbital. The FAD content of the liver mitochondrial and microsomal fractions were increased by either one shot administration or three successive daily administrations of phenobarbital. Similarly the flavokinase and FAD pyrophosphorylase activities also increased in the mitochondrial, microsomal and cytosol fractions. The authors have verified that activation of the FAD synthesizing system is induced by phenobarbital and suggest that the FMN and FAD contents are regulated not only by variations of flavin enzyme apoprotein, but also by changes in flavokinase and FAD pyrophosphorylase activities.

Adenosine Triphosphate↗