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Biomedical subjects

M Fujioka

Publications and source records attributed to M Fujioka.

At least 289 records · Page 16Linked to original sources
PubMed1980

[Manometric studies on asymmetry of lower esophageal sphincter in dogs (author's transl)].

Manometric pressure profile of the lower esophageal sphincter (LES) was measured with perfused 3-lumen tube (Sherwood Type I, Fr. 10) at 3 different directions at the same level in dogs. 1. Measurement in 8 mongrel dogs disclosed that LES pressure was significantly high at right anterior (2 o'clock) and left anterior (10 o'clock) directions compared with pressure at dorsal direction (6 o'clock). There was no statistically significant difference of LES length 3 different directions. 2. LES pressures and lengths were significantly increased and difference of LES pressures among 3 different directions was amplified by intravenous administration of 4 micrograms/kg/hr of Tetragastrin. 3. LES pressures and lengths were not affected by intravenous administration of 0.5 mg/kg/hr of Atropine sulfate. 4. LES pressures were preserved, but LES lengths were shortened by division of the phrenico-esophageal ligament. Difference of LES pressures among 3 different directions disappeared after this procedure. Division of the phrenico-esophageal ligament produced the "second" high pressure zone at directions of 2 and 10 o'clock. The present studies suggest that difference of LES pressures, or lengths in different directions is a product of anatomical structures of the hiatal muscle, and not of LES itself.

Animals↗
PubMed1979

Stereospecificity of hydrogen transfer in the saccharopine dehydrogenase reaction.

The stereospecificity of hydrogen transfer in the synthesis of saccharopine from alpha-ketoglutarate and L-lysine catalyzed by saccharopine dehydrogenase (N5-(1,3-dicarboxypropyl)-L-lysine: NAD oxidoreductase (L-lysine-forming), EC 1.5.1.7) was examined by using [4A-3H]- and [4B-3H]NADH. The enzyme showed the A-stereospecificity. The NMR analysis of the saccharopine prepared with [4"A-2H]NADH revealed that the label was incorporated into the C-2 of the glutaryl moiety.

Hydrogen↗
PubMed1979

Barotraumatic pneumothorax during cardiopulmonary bypass: a rare complication of open heart surgery.

In the absence of underlying lung disease, pneumothorax is a rare complication of open heart surgery in patients on cardiopulmonary bypass. However, barotraumatic pneumothoraces may be induced by manually applied endotracheal tube positive pressure to prevent air emboli from the left heart during open heart surgery. Two patients in whom barotraumatic pneumothoraces occurred during cardiopulmonary bypass and open heart surgery are reported.

Cardiopulmonary Bypass↗
PubMed1979

Radiographic evaluation of adenoidal size in children: adenoidal-nasopharyngeal ratio.

Adenoidal-nasopharyngeal ratios (AN ratios) obtained by simple linear measurements from lateral skull radiographs are described. The AN ratio reliably expresses adenoidal size and patency of the nasopharyngeal airway. The validity of the ratio as an indicator of adenoidal size was determined by evaluation of measurements of radiographs of 1,398 infants and children and comparison with a subjective visual assessment made by experienced observers in 92 patients. An AN ratio greater than 0.80 was present in 34 of 36 patients (94%) subjectively judged to have enlarged adenoids.

Adenoids↗
PubMed1978

Purification and characterization of saccharopine dehydrogenase from baker's yeast.

Saccharopine dehydrogenase (N6-(glutar-2-yl)-L-ly-sine:NAD oxidoreductase (L-lysine-forming)) from baker's yeast was purified to homogenicity. The overall purification was about 1,200-fold over the crude extract with a yield of about 24%. The purified enzyme had a sedimentation coefficient (S20,w) of 3.0 S. The molecular weight determinations by sedimentation equilibrium, Sephadex G-100 gel filtration, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis gave a value of about 39,000 and, therefore, saccharopine dehydrogenase is a single polypeptide chain enzyme. A Stokes radius of 27 A and a diffusion constant of 7.9 X 10(-7) cm2 s-1 were obtained from Sephadex gel filtration chromatography. The enzyme had a high isoelectric pH of 10.1. The NH2-terminal sequence was Ala-Ala----. The enzyme possessed 3 cysteine residues/molecule; no disulfide bond was present. Incubation of saccharopine dehydrogenase with p-chloromercuribenzoate or iodoacetate resulted in complete loss of enzyme activity. Whereas the coenzyme and substrates were ineffective in protecting from inactivation by p-chloromercuribenzoate, iodoacetate inhibition was protected by excess coenzyme.

Amino Acids↗
PubMed1978

67Ga-citrate scanning in hypernephroma.

67Ga scanning was performed in 26 patients with hypernephroma (17 with only a primary lesion of hypernephroma, 4 with both primary and metastatic lesions, 2 with hypernephroma and pyelonephritis, and 3 with only a metastatic lesion after nephrectomy). In patients with primary lesions alone, the positive finding rate by 67Ga scanning was low (26%), and in metastatic lesions that by scanning was high (86%). The practical conclusions are as follows: 67Ga scanning is of littel use as a diagnostic aid in primary lesion of hypernephroma, but may be useful in case with metastases with inflammatory disease.

Adenocarcinoma↗
PubMed1978

Enzymic and chemical synthesis of epilson-N-(L-propionyl-2)-L-lysine.

Pyruvate was shown to act as an oxo acid substrate in the reverse direction of saccharopine dehydrogenase [epsilon N-(L-glutaryl-2)-L-lysine: NAD oxidoreductase (L-lysine-forming)] reaction. The enzymic condensation product of lysine and pyruvate was isolated and identified as epsilon-N-(L-propionyl-2)-L-lysine by comparison with the synthetic compound. A method for the chemical preparation of diastereoisomers of epsilon-N-(propionyl-2)-L-lysine is also described.

Lysine↗
PubMed1978

The reaction of pyruvate with saccharopine dehydrogenase.

The preceding paper in this journal has reported that pyruvate could be substituted for 2-oxo-glutarate as a substrate of saccharopine dehydrogenase [epsilon-N-(L-glutaryl-2)-L-lysine:NAD oxidoreductase (L-lysine-forming) in the direction of reductive condensation. In the present communication, the kinetic mechanism of saccharopine dehydrogenase reaction with NADH, L-lysine and pyruvate as reactants is reported. The results of initial velocity study, inhibition studies with lysine analogs and a reaction product, NAD+, are consistent with an ordered mechanism with the coenzyme binding first and pyruvate last. The reaction mechanism is at variance with that of the normal reaction in which 2-oxoglutarate is the substrate, in that the order of addition of the amino and oxo acid substrates is reversed. This fact suggests that there exists a small degree of randomness in the binding of amino and oxo acid substrates. From a product inhibition study, NAD+ was shown to be the last reactant released. Saccharopine [epsilon-N-(L-glutaryl-2)-L-lysine] was found to act as a potent dead-end inhibitor of the condensation reactions (of lysine and 2-oxoglutarate, and of lysine and pyruvate) by forming an abortive E. NADH. saccharopine complex.

Kinetics↗