Search PubMed⌕ Search

Biomedical subjects

H Sawada

Publications and source records attributed to H Sawada.

At least 541 records · Page 30Linked to original sources

Three-dimensional observation on muscular tissues.

Striated muscle cells of frog sartorius and smooth muscle cells of guinea pig taenia coli were observed three-dimensionally by field emission type scanning electron microscope (FE-SEM) and freeze-fracture deep-etching replica (FFDE) method. By tearing at different preparative stages, various cellular structures appeared on SEM: the outer surface of cells, the inner surface of plasmalemma, and the interior of cells. On the inner surface of the plasmalemma of striated muscle, many caveolae, membranous structures and fine filaments were observed. Inside the cells myofibrils showed the characteristic banding pattern and on the thick filaments, a periodicity of 40 nm was observed. Along the myofibril, T-tubules and sarcoplasmic reticulum were seen with their regional differentiations. In smooth muscle cells, on the inner surface of the plasmalemma there were many caveolae, bundles of filaments and endoplasmic reticulum. The central part of smooth muscle cells were occupied by their nucleus, many microtubules, mitochondria and rough surfaced endoplasmic reticulum. By the FFDE method, observations on finer details were added to the SEM studies, including lateral projections of myosin filaments in striated muscles and fine filaments connecting thin myofilaments in smooth muscle cells. In the terminal cistern of the sarcoplasmic reticulum, networks composed of granular materials were observed.

Animals↗

Effects of anticancer platinum compounds on Escherichia coli strains with normal and defective DNA repair capacity.

The effect of anticancer platinum compounds on isogenetic strains of Escherichia coli with normal or defective DNA repair capacity were studied. Cisdichlorodiammineplatinum (II) causes DNA damage that is repairable by the repair systems of bacteria, and the DNA lesion becomes mutational when processed by the excision repair system. Dinitrato (1R, 2S-cyclohexanediamine) platinum (II) exhibits similar killing activity on E. coli strains with both normal and defective DNA repair capacity. Thus, this compound may cause DNA damage that cannot be repaired by bacteria, or its killing activity may be due to effects other than DNA damage.

Antineoplastic Agents↗

A possible functional relationship between microsomal aromatic aldehyde-ketone reductase and hexose-6-phosphate dehydrogenase.

Aromatic ketone reductase activity of microsomes showed a unique cofactor requirement: Addition of NADP and glucose-6-phosphate was as effective as that of an artificial NADPH generating system, whereas NADPH alone served as a cofactor less efficiently. Microsomal aromatic ketone reductase, purified partially from guinea pig liver microsomes after solubilization with Triton X-100, reduced 5 beta-dihydrotestosterone, aromatic aldehydes, and ketones with NADPH as a cofactor. However, addition of hexose-6-phosphate dehydrogenase, purified from the same source, as an NADPH generator produced about 2 times higher activity than that of yeast glucose-6-phosphate dehydrogenase or NADPH alone.

Alcohol Oxidoreductases↗

Antibody response following rubella immunization analyzed by HLA types.

Possible association between HLA antigens and antibody response to rubella vaccine was examined in 71 seronegative adult females, aged from 18 to 23, immunized with QEF vaccine. High responders (HAI antibody titer greater than or equal to 1:32) with HLA-B15 were significantly higher in frequency than those without HLA-B15 (p < 0.05). On the other hand, subjects with HLA-A9 had a tendency toward low immune responsiveness, including all the three non-responders. These results suggest that the antibody response to rubella vaccine may be influenced by the host-genetic factors relating to HLA antigens.

Adolescent↗

Reductases for aromatic aldehydes and ketones from rabbit liver. Purification and characterization.

Four aldehyde reductases, F1, F2, F3, and F4, were isolated from rabbit liver cytosol to homogeneity by various chromatographic techniques. F2 is an aldehyde reductase with a molecular weight of 32,000, which resembled aldehyde reductases of human liver and pig kidney in properties. It was inhibited in a noncompetitive way by alpha-ketoglutarate and oxaloacetate with Ki values of 4 x 10(-5) M. The other three enzymes were NADPH-dependent aromatic aldehyde-ketone reductases. F1 and F3 were monomeric enzymes with molecular weights of 38,000 and 29,000, respectively. F4 showed a molecular weight of 78,000 on gel filtration, but sodium dodecyl sulfate gel electrophoresis revealed two different subunits with molecular weights of 26,000 and 24,000. The molar ratio of NADPH : F1, F2, or F3 binding was 1 : 1, whereas that of NADPH:F4 binding was 3 : 1. The number of thiol groups in order molecule of F1, F2, F3, and F4, was 4, 4, 4, and 5, respectively. The enzyme activity of F3 was inhibited by addition of an equal mole amount of PCMB. Only F4 was inhibited by metal chelating agents. F1 also catalyzed the interconversion of 3(17)-keto and 3(17) beta-hydroxysteroids, whereas F3 catalyzed oxidoreduction of some 3 alpha-hydroxysteroids of the 5 alpha-series. These results suggest that F1 and F3 are 3(17) beta-hydroxysteroid dehydrogenase and 3 alpha-hydroxysteroid dehydrogenase, respectively. Endogenous substrates for F4 could not be identified in this work. F1 showed the lowest Km value for reduction of aldehydes and ketones among the four reductases. It has been suggested that F1 is the primary enzyme responsible for the reduction of endogeneous aldehydes and xenobiotic aldehydes and ketones in vivo.

Aldehyde Oxidoreductases↗