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Biomedical subjects

H Maeda

Publications and source records attributed to H Maeda.

At least 1,423 records · Page 79Linked to original sources
PubMed1977

Endogenous carbon monoxide production in alloxanized rats.

The endogenous production of carbon monoxide (Vco) in thirty-three diabetic rats induced by alloxan and in fifteen normal rats was measured by serial determinations of the expired carbon monoxide and of the increase of carbon monoxide in the blood during rebreathing in a closed system. Vco (mean +/- S.E., micronl/250g/hr) in the group of alloxanized rats 24, 48, 72, 96, 120 and over 144 hours after the alloxan injection was 6.2 +/- 2.9, 8.4 +/- 2.1, +/- 1.8, 10.7 +/- 3.5, 16.4 +/- 2.0 and 16.5 +/- 2.2, respectively, whereas it was 5.9 +/- 0.4 for the control. This indicates that the alloxanized group maintaining a high blood sugar level for over 120 hours has a three-fold higher Vco than the control.

Animals↗
PubMed1977

Histotoxic properties of carbon monoxide in the living organ I. Fluorometry of oxidation-reduction state of the rabbit kidney in situ.

Effect of carbon monoxide on the redox state and blood flow in the renal cortex of the rabbit was examined by the fluorometric method. By a short-period (1-3 min) inhalation of CO in concentrations over 1%, the following were revealed: (1) Reduced pyridine nucleotide was increased, (2) oscillatory change of the reduced pyridine nucleotide, which is characteristic for the histotoxic reaction, developed, and (3) extent of the fluorescence changes tended to be in proportion to the concentration of CO, but no change was caused by inhalation of CO in lower concentrations (0.1%, 0.5%) even if the inhalation was continued for 30 min. As to the blood flow, CO in concentrations over 0.5% decreased it, whereas anoxia due to nitrogen increased it. Some implications were discussed from toxicological points of view on the results obtained.

Animals↗
PubMed1976

Kinetics of dimerization of the variable fragment of the Bence-Jones protein Au.

The dimerization of the variable fragment of the Bence-Jones protein Au was examined in phosphate buffers at pH 6.8-6.9 And ionic strength of 0.1 M or 0.2 M at 20 degrees C. The dimerization constant was about 1 X 10(5) M-1. The reaction enthalpy was positive and the process was entropy driven. The association and dissociation rate constants were 9 X 10(6) M-1 s-1 and 1.5 X 10(2) s-1 respectively. Temperature-jump experiments exhibited the presence of two isomers of the dimer, which are present at equilibrium in a ratio of about 1:1. Isomerization occurred with a half-life of about 0.1 s.

Bence Jones Protein↗