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Biomedical subjects

Y Terano

Publications and source records attributed to Y Terano.

44 records · Page 3Linked to original sources
PubMed1987

Purification and characterization of two constitutive cytochromes P-450 (F-1 and F-2) from adult female rats: identification of P-450F-1 as the phenobarbital-inducible cytochrome P-450 in male rat liver.

Two hepatic microsomal cytochromes P-450, P-450F-1 and P-450F-2 were purified to electrophoretic homogeneity from untreated adult female rats by high-performance liquid chromatography (HPLC) with anion-exchange, cation-exchange, and hydroxyapatite columns. Cytochromes P-450F-1 and P-450F-2 were not adsorbed with the anion-exchange column, but were retained on a cation-exchange column and were separated poorly. These forms separated on hydroxyapatite HPLC. The molecular weights of cytochromes P-450F-1 and P-450F-2 were 50,000 and 49,000, respectively. The absolute spectrum of the oxidized forms indicated that they had the low-spin state of heme, and the CO-reduced spectral maxima of cytochromes P-450F-1 and P-450F-2 were at 450 and 448 nm, respectively. Both forms catalyzed the N-demethylation of benzphetamine and had low catalytic activity for 7-ethoxycoumarin. Cytochrome P-450F-1 had low 2 alpha-hydroxylation activity toward testosterone. Cytochrome P-450F-2 had low 15 alpha-hydroxylation activity. On the basis of these results and those of NH2-terminal sequence analysis, cytochrome P-450F-2 seemed to be the typical female-specific cytochrome P-450. The NH2-terminal sequence of cytochrome P-450F-1 was identical to that of cytochrome P-450PB-2 purified from hepatic microsomes of male rats treated with phenobarbital. Cytochromes P-450F-1 and P-450PB-2 had identical chromatographic properties, minimum molecular weight, spectral properties, and peptide maps. Furthermore, the antibody to phenobarbital-inducible cytochrome P-450PB-2 gave a single immunoprecipitin band with cytochrome P-450F-1 by Ouchterlony double-diffusion analysis.

Amino Acid Sequence↗
PubMed1987

Production and characterization of monoclonal antibodies to human tumor necrosis factor.

Five stable hybridoma cell lines secreting antibodies to recombinant human tumor necrosis factor (TNF) were established. All monoclonal antibodies belong to the IgG1 subclass. One monoclonal antibody (MAB) (designated as 3B10) neutralizes the L929 cytotoxic activity of natural and recombinant human TNF. Other MABs bind to human TNF but do not neutralize cytotoxic activity. A sandwich enzyme immunoassay specific to human TNF molecule has been developed using 3B10. This assay measures only biologically active human TNF molecules and is as sensitive as a bioassay which measures the cytotoxic activity on L929 cells. These results show that 3B10 is quite useful in studying the biological functions of TNF.

Animals↗
PubMed1986

Circulating factor with ouabain-like immunoreactivity in patients with primary aldosteronism.

Circulating factor with ouabain-like immunoreactivity was studied in patients with primary aldosteronism. Anti-ouabain antibody was prepared from specific pathogen-free rabbits. In the plasma of patients with primary aldosteronism, the level of a factor with ouabain-like immunoreactivity was 2.59 +/- 1.39 pmol ouabain equivalent/ml plasma. This value was significantly (p less than 0.05) higher than that of age-matched normotensive subjects, 1.06 +/- 0.86 pmol ouabain equivalent/ml plasma. The plasma level of ouabain-like immunoreactivity correlated significantly (p less than 0.05) with blood pressure. These results indicate that the factor with ouabain-like immunoreactivity may play a pathophysiological role in the maintenance of the high blood pressure observed in patients with primary aldosteronism.

Antibody Affinity↗
PubMed1984

Distribution of the histaminergic neuron system in the central nervous system of rats; a fluorescent immunohistochemical analysis with histidine decarboxylase as a marker.

The distribution of histidine decarboxylase-like immunoreactivity (HDCI) in the rat central nervous system was studied by the indirect immunofluorescence technique. HDCI cell bodies were concentrated in the posterior hypothalamic area, such as in the tuberal magnocellular nucleus, caudal magnocellular nucleus, posterior hypothalamic nucleus and lateral hypothalamus just lateral to the fasciculus mammillothalamicus at the level of the posterior hypothalamic nucleus. Extensive networks of HDCI fibers of various densities were found in many areas of the brain; they were particularly dense in the hypothalamus but were also found in the following areas: rostrally in the cerebral cortex, olfactory nuclei, medial amygdaloid nucleus, n. tractus diagonalis, and bed nucleus of the stria terminalis, and caudally in the central gray matter of the midbrain and pons, auditory system, n. vestibularis medialis, n. originis nervi facialis, n. parabrachialis, n. commissuralis, n. tractus solitarii, and n. raphe dorsalis.

Animals↗
PubMed1983

Evidence for the presence of a histaminergic neuron system in the rat brain: an immunohistochemical analysis.

Histamine-containing cells in rats were identified by indirect immunofluorescent histochemistry using an antibody raised against histidine decarboxylase (HDC), the enzyme forming histamine, which was purified from fetal rat liver. HDC-like immunoreactive (HDCI) structures could be detected in the brain as well as in peritoneal mast cells and basal-granulated cells in deep crypts of the gastric mucosa of rats. Numerous HDCI neurons were found in the posterior hypothalamic area and HDCI nerve fibers with a varicose appearance of fluorescence were widely distributed in various regions of the brain.

Animals↗