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Biomedical subjects

T Seno

Publications and source records attributed to T Seno.

At least 145 records · Page 8Linked to original sources
PubMed1979

Mutagenic activation of 2-acetylaminofluorene by guinea-pig liver homogenates: essential involvement of cytochrome P-450 mixed-function oxidases.

2-Acetylaminofluorene (AAF) was highly mutagenic to Salmonella typhimurium strain TA98, when activated by a liver post-mitochondrial supernatant fraction (S9 fraction) from guinea-pigs, in spite of the resistance of this species to AAF carcinogenesis and the low capacity of the liver of this species for N-hydroxylation of AAF. The mutagenicity was comparable to or higher than that resulting from activation by mouse- or rat-liver S9 fraction, and was not enchanced by treatment with cytochrome P-450 inducers, a combination of phenobarbital and 5,6-benzoflavone. In an attempt to understand this unexpected result we examined whether a cytochrome P-450 mixed-function oxidase system participated in the mutagenic activation of AAF by guinea-pig liver, as it does in the case of mouse liver. The mutagenic activation was: (1) completely dependent on the addition of a co-factor, NADPH, to the mutation assay system, (2) completely suppressed by antiserum against NADPH--cytochrome c reductase, and (3) sensitive to a cytochrome P-450 inhibitor, 7,8-benzoflavone. These results indicate that the cytochrome P-450 enzyme system is essentially involved even in the mutagenic activation of AAF by guinea-pig-liver S9 fraction. Based on both the present and other data, the mechanism of the mutagenic activation is discussed to explain the observed high mutagenic potential of AAF in the presence of guinea-pig-liver S9 fraction.

2-Acetylaminofluorene↗
PubMed1979

Differential effect of a microsomal deacetylase inhibition on the mutagenicity in Salmonella typhimurium of 2-acetylaminofluorene by liver homogenates of guinea pigs, mice and rats.

The effect of paraoxon, a microsomal deacetylase inhibitor, on the mutant genicity of 2-acetylaminofluorene (AAF) by liver homogenates was compared between the AAF carcinogenesis-resistant guinea pigs and the susceptible mice and rats. The mutagenicity of AAF was mostly abolished by paraoxon, not only in the 3 kinds of untreated animals but also in guinea pigs treated with a combination of phenobarbital and 5,6-benzoflavone, whereas about 50% of the mutagenicity was resistant to paraoxon in treated mice and rats. We suggest that microsomal deacetylase activity is crucially involved in the mutagenic activation of AAF by guinea pig liver homogenates, while the enzyme activity other than the deacetylase activity is also important in the activation by liver homogenates from treated mice or rats.

2-Acetylaminofluorene↗
PubMed1978

Interaction of Escherichia coli glutaminyl-tRNA synthesis with noncognate tRNA's.

Several noncognate tRNA's from Escherichia coli were mischarged with glutamine by E. coli glutaminyl-tRNA synthetase if dimethylsulfoxide was present in the reaction mixture. Kinetic analysis of the mischarging revealed that dimethyl sulfoxide stimulated the misacylation by affecting the maximum velocity. Several noncognate tRNA's were shown to interact with glutaminyl-tRNA synthetase as measured by their ability to protect the enzyme against thermal inactivation or to replace cognate tRNA in stimulating glutamine-dependent ATP-PPi exchange reaction. These tRNA's, however, did not coincide with those which were mischargeable with glutamine.

Amino Acids↗
PubMed1978

An example of naturally occurring anti-Kell (K1) in a Japanese male.

'Naturally occurring' anti-Kell (K1) was found in a Japanese male who has never received a transfusion. The antibody agglutinated K:1 cells suspended in saline at 4 and 22 degrees C as well as cells suspended in albumin and treated with proteolytic enzymes.

Blood Group Antigens↗
PubMed1972

Is there a discriminator site in transfer RNA?

We determined the nature of the fourth nucleotide from the 3'-end of several Escherichia coli tRNAs, and tabulated these results with the same data for all known tRNA sequences. We find a striking constancy of the fourth nucleotide in tRNAs specific for a given amino acid. Furthermore, tRNAs specific for chemically related amino acids are very likely to have the same nucleotide at the fourth position. One possible explanation for these regularities is the "discriminator" hypothesis: The code by which tRNA is recognized by its cognate aminoacyl-tRNA synthetase is logically hierarchical, with the fourth nucleotide serving as a primary "discriminator" site to subdivide the tRNAs into groups for recognition purposes. Each such group could have its own recognition code, or could be further subdivided by a secondary discriminator site. According to this hypothesis, chemically similar amino acids have the same discriminator nucleotide because they evolved from a single set of related amino acids indistinguishable to a primitive system. There are other possible explanations for the observed regularities at the fourth nucleotide. For example, it is conceivable that the position is used for a direct physical interaction with the amino acid in the charging process, and chemically similar amino acids naturally select the same nucleotide. Further experiments can be expected to clarify this question.

Acylation↗