[Thymus related tumor--classification and therapy (author's transl)].
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Biomedical subjects
Publications and source records attributed to H Wada.
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Glutamic oxaloacetic transaminase isozymes were purified simultaneously to homogeneity from rat liver with high yields. Three subforms of mitochondrial isozyme and three subforms of cytosolic isozyme were separated by chromatography on CM-Sephadex and electrophoresis on polyacrylamide gel. The general enzymatic properties of the purified isozymes such as their kinetic parameters, isoelectric points, molecular weights, amino acid compositions, NH2-terminal amino acid sequences and COOH-terminal amino acids were determined. Most of these properties of the isozymes are similar to those of the corresponding isozymes from other sources, such as rat brain and pig and human heart. In amino acid compositions, cytosolic isozyme from rat liver has more proline and glycine and less arginine, threonine and leucine than pig heart cytosolic isozyme; the mitochondrial isozyme has more glutamic acid and glycine and less serine than the corresponding pig heart isozyme. The NH2-terminal amino acid sequences of GOT isozymes from rat liver were identical with those of the GOT isozymes from pig heart up to the 10th residues except for the 5th residues. The subforms of mitochondrial isozyme from rat liver were generated on storage at 4 degrees C for 4-8 weeks.
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A simple method for the simultaneous determination of noradrenaline, dopamine and serotonin using a short column of Amberlite CG-50 is described. Noradrenaline and dopamine were eluted from the column with phosphate buffers containing 1.5 and 4.0% boric acid, respectively, and then serotonin was eluted with 1.0 N HCl. Catecholamines were determined by a modification of the ethylenediamine condensation method using potassium ferricyanide as oxidant and isobutanol for extraction of the fluorophores. Serotonin was measured by the acidic o-phthalaldehyde method. The method was applied to the simultaneous determination of noradrenaline, dopamine and serotonin in discrete regions of rat brain.
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The effect of purothionin, a peptide isolated from wheat flour, on adrenal medullary cells was examined in perfused bovine adrenal glands. Addition of purothionin (4 microgram/ml) to the perfusion fluid caused the release of cytoplasmic glutamic oxaloacetic transaminase (c-GOT), DOPA decarboxylase (DDC) and magnesium ions, which are present in the cytoplasmic fraction of adrenal medulla, but not the release of dopamine-beta-hydroxylase (DBH) or mitochondrial glutamic oxaloacetic transaminase (m-GOT), which are located in the particulate fraction. These results suggest that purothionin makes small pores in the cytoplasmic membranes of bovine adrenal medullary cells, resulting in the leakage of the cytoplasmic proteins and ions from the cells.
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