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Biomedical subjects

T Ando

Publications and source records attributed to T Ando.

At least 667 records · Page 37Linked to original sources
PubMed1981

Separation of cytochromes c by reversed-phase high-performance liquid chromatography.

Six kinds of cytochrome c of different origin, i.e., bovine, chicken, dog, horse, rabbit and tuna, were subjected to separation by reversed-phase high-performance liquid chromatography on three commercial packing materials; octadecyl-, octyl- and cyanoalkyl-silicas. The effects of reversed-phase material, mobile phase and temperature on the separation of cytochromes c were examined. The parameters of the mobile phase were the organic modifier, the pH, the salt concentration and additives. Under optimal conditions, five of the six cytochromes c were resolved in 10 min. The relative retention values cannot be explained in terms of the relative lipophilicities of the side-chains of the amino acid residues.

Animals↗
PubMed1981

Chromosomal loci of genes controlling site-specific restriction endonucleases of Bacillus subtilis.

We constructed transformation of B. subtilis 168 which acquired genes for site-specific restriction endonucleases. These endonucleases originated from various strains of B. subtilis and were classified into five groups based on the specificity of the sequences recognized by the enzymes. We examined the loci of genes for site-specific restriction endonucleases belonging to different groups: hsrE determined Endo. R. Bsu1231 (I), hsrB Endo.R.Bsu1247(I), hsrR Endo.R.BsuR and hsrC Endo.R.Bsu-1247(II). One gene, hsrE, was located between sacA and purA by transduction crosses with phage PBS1, and another gene, hsrB, between hsrE and purA. Genes hsrR and hsrC had been suggested to be allelic or closely linked by previous studies with transformation. We located hsrR and hsrC between purB and tre. Our previous observation and this study show that B. subtilis 168 has at least three independent loci on the chromosome for four genes for site-specific restriction endonucleases in addition to the locus for the original restriction activity (Bsu168-specific restriction) of strain 168.

Bacillus subtilis↗
PubMed1980

Bacillus subtilis-phage phi 1 overcomes host-controlled restriction by producing BamNx inhibitor protein.

Bacillus amyloliquefaciens N produces two restriction enzymes, BamNI and BamNx. Subtilis-phage phi 1 is strongly restricted by BamNx. We isolated phi 1 rH, a mutant of phage phi 1, which overcame the BamNx-restriction by producing inhibitor. This inhibitor inactivated BamNx specifically and reversibly. The inhibitor directly interacted with BamNx and the inactivation might be the result of formation of a binary complex. The inhibitory activity was sensitive to treatment with trypsin. The molecular weight of the inhibitor protein was estimated to be approximately 20,000 daltons by gel filtration.

Bacillus subtilis↗
PubMed1980

A new one-step method for the cytochemical localization of ouabain-sensitive, potassium-dependent p-nitrophenylphosphatase activity.

A new one-step method for the light and electron microscopic localization of the ouabain-sensitive, K-dependent p-nitrophenylphosphatase (K-NPPase) activity of the Na-K-ATPase complex is introduced. The incubation medium contains p-nitrophenylphosphate (NPP) as substrate, lead citrate as the capture reagent, and dimethylsulfoxide (DMSO) as an activator. It is usable at the optimal pH of the K-NPPase, which is about pH 9.0 in the presence of 25% of DMSO. The effects of fixation, lead concentration, and DMSO on the enzyme activity were studied using rat kidney as a test tissue. The fixation of tissues in a mixture of 2% paraformaldehyde and 0.5% glutaraldehyde for 60 min at 0 degrees--4 degrees C preserved 45% of the enzyme activity. In the absence of DMSO, lead citrate (4.0 mM) caused 82% inhibition of the enzyme activity in fixed tissue. However, the addition of DMSO (25%) caused about 3-fold activation of the remaining activity. Cytochemical demonstration of the ouabain-sensitive K-NPPase activity was successfully made by this method at both light and electron microscopic levels.

4-Nitrophenylphosphatase↗
PubMed1980

Cranioplasty utilizing a preserved autogenous bone flap coated with acrylic resin.

Cranioplasty utilizing a resin-coated preserved autogenous skull flap was devised and used in 36 cases, 14 of them being followed up radiologically. It has been confirmed that this method is advantageous in that it repairs the skull defect satisfactorily both from surgical and cosmetic points of view. Furthermore this method causes no anxiety to the patient because of the autogenous origin of the bone flap. We recommend this method for cranioplasty when an autogenous bone flap is preserved.

Adolescent↗