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Biomedical subjects

T Mizukami

Publications and source records attributed to T Mizukami.

At least 91 records · Page 5Linked to original sources

Transplantation of cryopreserved pancreatic islets into the portal vein.

Pancreatic islet cells of rats obtained by the collagenase digestion method were preserved from 7 to 10 days at -80 degrees C in a deep freezer or at -196 degrees C in liquid nitrogen with Dulbecco modified Eagle's medium, supplemented with 10% or 20% DMSO (dimethyl sulfoxide); thawing was performed in a 37 degree C water bath. Cryopreserved islets were morphologically almost intact, and possessed approximately 50% of the insulin secretion activity of the control groups. About 300 pancreatic islets preserved at -196 degrees C with 20% DMSO were transplanted into the portal veins of streptozotocin-induced diabetic rats. Rats recovered from the diabetic state, and the normalized condition was maintained up to 20 weeks, although 4 weeks were needed before blood and urine glucose reached normal levels after transplantation. Intact B cells were found in the transplanted islet cell masses in the liver of the recipients, but B cells of the recipient's pancreases (streptozotocin-treated rats) showed a marked decrease, as well as degenerative changes.

Animals↗

A physical map of the genome of the Bacillus subtilis temperate phage rho 11.

A cleavage map of Bacillus subtilis temperate phage rho 11 was constructed with restriction endonucleases SalI, BamHI and BglII, which cut the genome into 6, 7 and 21 fragments, respectively. The molecular weight of the rho 11 genome was calculated to be 78 x 10(6). Among other endonucleases tested, PvuII, EcoRI and XbaI cleaved the genome into more than 25 fragments, while HaeIII, StuI, BalI and BamNx did not cut the genome at all. The rho 11-coded thymidylate synthetase gene, thyP11, was found to be located in the SalI-D fragment, which was in the central region of the genome.

Bacillus subtilis↗

Studies of the action pattern of an alpha-amylase from Streptomyces praecox NA-273.

An alpha-amylase [EC 3.2.1.1] from Streptomyces praecox was purified and its characteristic action, the conversion of maltotriose (G3) to maltose (G2) without appreciable formation of glucose (G1), was investigated. Isoelectric focusing or the glycogen adsorption procedure was employed after chromatography. Isoelectric focusing showed that the enzyme preparation after chromatographic separation comprises three isozymes. The preparation from the glycogen adsorption procedure showed the highest specific activity of any preparation of this enzyme ever obtained. Product analysis with uniformly labeled G3 revealed that at a high concentration (18 mM) of G3, much more G2 is produced than G1 (the product ratio G2/G1 is over 20), while at a lower concentration (10 microM) the reaction mixture was composed of nearly equimolar amounts of glucose and maltose. Based on the product analysis of reducing end-labeled G3 in addition to the above findings, the following conversion mechanism is proposed: Streptomyces alpha-amylase catalyzes transglycosylation to produce maltotetraose (G4) as a transient product which is immediately degraded into two molecules of G2 by a subsequent hydrolytic reaction, i.e., two molecules of G3 are converted into three molecules of maltose without appreciable formation of glucose.

Amylases↗

Studies on the substrate specificity of Taka-amylase A. XIII. Preparation of 6-deoxy-6-iodomaltooligosaccharides and their inhibitory action against Taka-amylase A1.

O-alpha-D-Glucopyranosyl-(1 leads to 4)-O-6-deoxy-6-iodo-alpha-D-glucopyranosyl-(1 leads to 4)-D-glucopyranose (6'-MT), O-alpha-D-glucopyranosyl-(1 leads to 4)-6-deoxy-6-iodo-D-glucopyranose (6-M), and O-6-deoxy-6-iodo-alpha-D-glucopyranosyl-(1 leads to 4)-D-glucopyranose (6'-M) were prepared and their inhibitory action against Taka-amylase A [EC 3.2.1.1, alpha-1, 4-glucan 4-glucanohydrolase, Aspergillus oryzae] was investigated. The inhibitor constants of 6'-MT and 6'-M were 10 mM and 54 mM, respectively, and both inhibitors showed mixed-type inhibition. 6-M scarcely inhibited the enzyme action.

Amylases↗

A comparative study of the contraceptive mechanism of the Cu-intrauterine device and the plastic-intrauterine device in rats.

After inserting the Cu-IUD and plastic-IUD into the horn of the uterus of rats, vaginal smears were daily observed for twelve estrus cycles, but no abnormal changes were noted. The female rats with the IUD were exposed to impregnation placing together with male rats. Neither the Cu-IUD nor the plastic-IUD affected copulation, and a complete contraceptive result was obtained in these rats. There were no significant differences in any effect examined between Cu-IUD and plastic-IUD groups. In order to investigate the influence of copper on the penetration of sperm, we placed the rats with the IUD under direct observation and then exposed them to natural copulation. By examining various sites of the reproductive organs 30 min after copulation, the hindrance of sperm migration by the Cu-IUD was confirmed.

Animals↗

The isolation and characterization of a lethal protein from Kintoki beans (Phaseolus vulgaris).

A lethal protein with hemagglutinating activity but without trypsin inhibitory activity was isolated from beans of Phaseolus vulgaris, cultiva, and Kintoki and proved homogeneous by ultracentrifugation, disc polyacrylamide gel electrophoresis, sodium dodesyl sulfate polyacrylamide gel electrophoresis and isoelectric focusing. The molecular weight was estimated to be 104, 000 by ultracentrifugal analysis and gel filtration on Sephadex G-200. The molecule dissociates into three identical subunits in the presence of 8 M urea or 0.1% sodium dodesyl sulfate. The amino acid composition was characterized by the high content of aspartic acid and the complete absence of methionine and cystine. The carbohydrate content was 8.1%; 5.0% mannose and 3.1% glucosamine. The addition of the lethal protein to a basal diet (0.4%) resulted in the intensive depression of the growth and finally in the death of rats. The intraperitoneal injection of 250 microgram per g body weight of mouse brought about an acute toxicity which caused death of all the injected mice.

Amino Acids↗