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Biomedical subjects

K Shimada

Publications and source records attributed to K Shimada.

At least 1,675 records · Page 93Linked to original sources
PubMed1972

Virus-specific ribonucleic acid in the nucleus and cytoplasm of rat embryo cells transformed by adenovirus type 2.

Nuclei were isolated from rat embryo cells transformed by adenovirus type 2. Nuclear and cytoplasmic virus-specific ribonucleic acids (RNA) were characterized and quantitated by deoxyribonucleic acid (DNA)-RNA hybrid formation with adenovirus DNA. The results indicate that most, if not all, virus-specific RNA molecules are synthesized in the cell nucleus and subsequently transported into cytoplasm where they degrade with a half-life of 1 to 2 hr. No difference in base sequences between nuclear and cytoplasmic virus-specific RNA species can be detected by hybridization competition experiment with viral DNA.

Adenoviridae↗
PubMed1972

[Intussusception].

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Intussusception↗
PubMed1971

Isolation of the gal repressor.

The repressor of the galactose operon of Escherichia coli has been partially purified and identified as a protein. Induction of a lysogen in which lambda was linked to the bacterial galR and lysine genes resulted in a large increase in the production of the gal repressor. Single-step purification by affinity chromatography, using the ligand p-aminophenyl-beta-D-thiogalactoside linked to beaded agarose, provided a convenient method of separating the gal repressor from other DNA-binding proteins. Binding of gal repressor to lambdapgal[(32)P]DNA was studied by assay of binding to a nitrocellulose filter. Interaction between gal repressor and lambdapgal DNA showed a high degree of specificity; the dissociation constant of the complex was estimated to be 1.0 x 10(-12) M. Unlabeled lambdapgal DNA competed for binding to gal repressor, but lambdaDNA and lambdah80dlac DNA did not. Fucose and galactose, which function as inducers of the galactose operon in vivo, produced one-half maximal inhibition of gal repressor-lambdapgal DNA binding at concentrations of 5 x 10(-5) M.

Chromatography↗