Biomedical subjects
Publications and source records attributed to I Suzuki.
Blue dextran at low concentrations (0.1-1 ng/ml) agglutinated human, mouse, rabbit and rat erythrocytes. This agglutination was inhibited by 10% calf serum, 0.5 mg/ml bovine albumin and 0.2 M sodium thiocyanate, and less effectively by 1.5 M potassium chloride, but not by 30-50 mM magnesium sulfate.
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Spores of Clostridium tetani germinated in liver broth with +580 mV as the starting Eh value, and those of Clostridium butyricum germinated in liver broth with an initial Eh of +400 mV regardless of the presence or absence of a liquid paraffin covering. Spores of Bacillus subtilis germinated in liver broth with--100 mV as the starting Eh value. Also, it was found that there are two ranges of starting Eh values for germination and vegetative growth of Cl. tetani, Cl. butyricum, and B. subtilis. In the first range these spores germinated and grew, but in the second range they only germinated and then died without outgrowth.
A bubble oxygenator (the TM or the OCVC oxygenator) has been produced with development efforts focused particularly on reduction of the nonphysiological characteristics of this type of oxygenator. The structural features of the apparatus are: (1) a reduction to the minimum of adequate priming volume, (2) an oxygen disperser designed to ensure evenly dispersed, uniform-sized bubbles, (3) a volume-control system for the oxygenating chamber (the OCVC system) based on extensive experimental oxygenation studies, and (4) an integrated double microfilter of the gravity-drainage type. Clinical features are: (1) ease of operation in perfusion, (2) reduction in hemolysis and postoperative blood loss, and (3) fewer complications associated with microemboli. Clinical use on over 200 infants and children proved generally very satisfactory. The background of its development is briefly described as are future modification plans.
Mechanism of ammonia oxidation was studied in the reconstituted system of Nitrosomonas membrane fraction plus the Nitrosomonas cytochrome c554. The cytochrome c554 was reduced by hydroxylamine, hydrazine, and ammonia and the reduced cytochrome was oxidized upon the addition of ammonia or carbon monoxide. The oxidation of carbon monoxide in the presence of hydroxylamine or hydrazine was studied as a possible assay method for ammonia hydroxylase where hydroxylamine or hydrazine was supplying the reducing power required for the hydroxylation of carbon monoxide. The stoichiometry of the reaction, Km values for substrates, and effects of pH and inhibitors were investigated. It is concluded that carbon monoxide, a competitive inhibitor for ammonia oxidation, is an alternate substrate for ammonia hydroxylase using the reduced cytochrome c554 as the reducing power.
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A glycoprotein, Aloctin A, which was isolated from Aloe arborescens Mill, markedly inhibits adjuvant arthritis in rats and carrageenin-induced edema in rats.
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Conditions essential for the preparation of active ammonia-oxidizing extracts of Nitrosomonas europaea were studied. The extracts were unstable during storage and required specific assay conditions for ammonia oxidation. Bovine serum albumin, spermine, or MgCl2 was required for ammonia oxidation and the concentration of phosphate determined the relative effectiveness of each activator, i.e., albumin being most effective in 0.1 M phosphate and spermine or MgCl2 at lower phosphate concentrations. Kinetic experiments showed a partial reduction of cytochrome c preceding the initiation of oxygen consumption due to ammonia oxidation.
The cell-free ammonia-oxidizing system of Nitrosomonas europaea was resolved into three major fractions: a membrane fraction containing cytochrome a1 and c-type cytochromes, a fraction with hydroxylamine-cytochrome c reductase and a cytochrome c fraction. The ammonia-oxidizing activity was reconstituted by the combination of these three fractions. The activity was more consistently reconstituted by adding Nitrosomonas cytochrome c554 to the membrane fraction. The hydroxylamine-cytochrome c reductase activity of the membrane fraction increased with the addition of cytochrome c554, but the oxidation of hydroxylamine to nitrite required a further addition of cytochrome c552. The ammonia oxidation by the membrane plus cytochrome c554 was affected by the concentration of phosphate and the addition of bovine serum albumin, spermine, or MgCl2.
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