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Biomedical subjects

K Matsuda

Publications and source records attributed to K Matsuda.

At least 631 records · Page 35Linked to original sources
PubMed1987

Cholinergic and VIPergic vasodilator actions of parasympathetic nerves on the thyroid blood flow in rats.

The present experiment was performed to investigate the effect of stimulating the parasympathetic superior laryngeal nerve (SLN) on thyroid blood flow and its mediator substances in urethane-chloralose anesthetized rats. Thyroid blood flow was measured by counting number of blood drops from a thin catheter inserted into the thyroid vein. SLNs were cut bilaterally and their peripheral portions were electrically stimulated. Electrical stimulations (intensity, 10 V; pulse duration, 0.5 ms) of SLNs increased thyroid blood flow in a frequency-dependent manner as stimulus frequencies increased from 2 to 40 Hz. The intravenous administration of atropine (0.5 mg/kg) reduced these responses, but did not abolish them. The basal secretion rate of vasoactive intestinal peptide (VIP) from thyroid glands in the resting state was nearly zero (0.25 +/- 0.14 pg/(kg.min)). SLN stimulation increased markedly the VIP secretion rate to 3.40 +/- 0.64 pg/(kg.min). The VIP secretion responses evoked by SLN stimulation remained in atropinized rats. Furthermore, exogenously applied VIP increased the thyroid blood flow dose-dependently. These results suggest that SLN stimulation increases the thyroid blood flow by dilating thyroid blood vessels via activation of cholinergic and non-cholinergic (probably VIP-containing) nerve fibers. Thus, these parasympathetic vasodilation systems may play a supplementary role in regulating the secretion of thyroid hormone by changing the thyroid blood flow in addition to the role of hormonal regulation by the thyroid stimulating hormone (TSH).

Animals↗
PubMed1987

Relationship between Candida albicans producing proteinase (CAPP) and its environmental pH--comparison with a case of trichophyton mentagrophytes.

Candida albicans produced a karatinolytic proteinase (KPase) or C. albicans producing proteinase (CAPP), a proposed new term for this enzyme, and Trichophyton mentagrophytes also produced KPase when cultivated in liquid medium containing human stratum corneum (HSC) as the nitrogen source, but were unable to do so when cultivated in sabouraud dextrose broth. Purified KPase from the culture supernatants of C. albicans had a molecular weight of 42,000 and an optimum pH at 4.0. The KPase was found to belong to the carboxyl proteinases group and its activity was strongly inhibited by pepstatin. Both fungi were able to grow by secreting KPase which digested HSC for nutrients. KPase from both fungi had high activity in each optimum pH, such as weakly acidic pH on C. albicans and neutral pH on T. mentagrophytes to adapt their surrounding environment by changing the environmental pH into their own optimum pH.

Candida albicans↗
PubMed1987

Two types of phosphorylase from etiolated soybean cotyledons.

Two types of phosphorylase [EC 2.4.1.1] from the etiolated soybean (Glycine max) cotyledons were separated by column chromatography on DEAE-Sephacel and further purified to apparent homogeneities. Molecular weights of the subunits were 100,000 and 113,000 for phosphorylases I and II, respectively. The native enzymes I and II were a dimer (200,000) and tetramer (450,000), respectively. Electrophoretic analysis by the Hedrick and Smith method indicated that the two phosphorylases were distinct proteins with no correlation. The apparent Km values for glucose 1-phosphate, glycogen, and maltoheptaose of enzyme I were 4.00 mM, 0.18 mg/ml, and 10.3 mM, respectively, while those values of enzyme II were 5.43 mM, 23.8 mg/ml, and 0.30 mM, respectively. The relative activity of enzyme I increased with increasing chain length of the substrate glucans, and waxy maize amylopectin was the best substrate among the 11 saccharides examined. For enzyme II, maltooligosaccharides with degree of polymerization (DP) 5-7 were the better substrates than amylose (DP 38) and glycogen. These results indicated that the soybean phosphorylases I and II have similar properties to a cytoplasmic and chloroplastic type of plant leaf enzyme, respectively.

Chromatography, DEAE-Cellulose↗
PubMed1987

Distribution of pancreatic secretory trypsin inhibitor in various human tissues and its inactivation in the gastric mucosa.

Considerable amounts of immunoreactive pancreatic secretory trypsin inhibitor were detected in lung, stomach, liver, pancreas, kidney, small intestine and ovary. Immunoreactive pancreatic secretory trypsin inhibitor content of surgically removed gastric mucosa was approximately seven times higher than that of gastric mucosa obtained at autopsy. The reduction in PSTI-immunoreactivity seen in a tissue extract of fresh gastric mucosa on 24 hours' incubation represented 9% of the original immunoreactivity in 10 mM Tris-HCl buffer, pH 7.4, at 37 degrees C. While, there was a more than 80% reduction in immunoreactivity on 12 hours' incubation at 37 degrees C at pH 4.0 or under more acidic conditions.

Female↗
PubMed1986

Purification and characterization of pancreatic secretory trypsin inhibitor in human gastric mucosa.

Immunoreactive pancreatic secretory trypsin inhibitor (PSTI) was purified to homogeneity from human gastric mucosa by gel chromatography, ion-exchange chromatography, and repeated reverse-phase high-performance liquid chromatography (HPLC). The molecular weight of the purified immunoreactive PSTI in human gastric mucosa was estimated to be 6000. The electrophoretical mobility of purified PSTI was identical with that of the main component of PSTI in human pancreatic juice. It consisted of 56 amino acids and had the same amino acid composition as PSTI in pancreatic juice. It inhibited bovine pancreatic trypsin stoichiometrically, and did not inhibit porcine pancreatic kallikrein or elastase. Heat treatment of immunoreactive PSTI in gastric mucosa showed the same inactivation curve of immunoreactivity as that of pancreatic juice PSTI.

Amino Acids↗
PubMed1986

Determination of mitochondrial aspartate aminotransferase in serum.

Two specific and sensitive immunoassay methods for the determination of mitochondrial aspartate aminotransferase (m-AST) are described. One is a sandwich enzyme immunoassay which measures immunologically active m-AST using polystyrene balls coated with anti-m-AST antibody and peroxidase-labelled anti-m-AST antibody as the second antibody. The detection limit of this assay was 10 micrograms/l. The other is a paper disk method which measures catalytically active enzyme bound to anti m-AST antibody-conjugate paper disks. The calibration curve was linear up to 250 U/l. These assay methods were used to monitor the level of m-AST in serum. From measurements obtained by both methods, the correlation between the concentration of m-AST protein and its activity was poor (liver diseases, r = 0.539; myocardial infarction, r = 0.774) confirming that an inactive form of m-AST exists in serum, and that the specific activity of serum m-AST differs in individual diseases.

Animals↗
PubMed1986

Development of a radioimmunoassay for human deoxyribonuclease I.

A reliable radioimmunoassay (RIA) for human deoxyribonuclease I (DNase I) is described. Using delayed addition of tracer antigen, the method is sensitive (9.5 reproducible and specific. A good parallel relationship was observed between the standard curve and dilution curves for human urine and human pancreatic juice. G-actin, a naturally occurring DNase I inhibitor, caused no change in the immunoreactivity of DNase I. In healthy individuals, aged 11-90 yr, the mean serum DNase I was 18.4 ng/ml (SD 6.7 ng/ml). Increased serum DNase I occurred in patients with acute pancreatitis, renal failure, and in about one-third of patients with various malignant tumors.

Actins↗
PubMed1986

Synthesis of protected purpurosamine B and 6-epipurpurosamine B.

In relation to the synthesis of antipseudomonal drugs, namely, gentamicin C2 and 3-de-O-methylsporaricin A, a protected purpurosamine B (15) and 6-epipurpurosamine B (13) were synthesized. The key intermediate, methyl 2,3,4,7- tetradeoxy-6-O-(methylsulfonyl)-2-phthalimido-beta-L-lyxo-++ +heptopyranoside (8), was obtained in 48% yield by Grignard addition to methyl 2,3,4-trideoxy-2-phthalimido-alpha-D-erythro-hexodialdo-1,5-pyrano side (7) proceeding in accordance with Cram's chelate rule, followed by methylsulfonylation. From 8, compound 15 was readily obtained by introduction of the azide group with inversion of configuration at C-6. Compound 13 was obtained by introduction of the azide group with retention of configuration.

Anti-Bacterial Agents↗
PubMed1986

Immunochemical characterization of hepatitis B e antigen subtypes, HBeAg/1 and HBeAg/2, in sera of hepatitis B virus carriers.

The interrelation between HBeAg subtypes, HBeAg/1 and HBeAg/2, in sera was examined immunochemically. The detection of HBeAg subtypes in immunodiffusion (ID) depended upon the amount of HBeAg determined by reversed passive haemagglutination (RPHA), ie, the titres of HBeAg in sera positive for both HBeAg/1 and HBeAg/2, positive for only HBeAg/1 and negative for both HBeAg/1 and HBeAg/2 were 2(9.8) +/- 1.5, 2(7.0) +/- 1.6, and 2(5.6) +/- 1.3, respectively. When the sera belonging to the latter two groups were concentrated up to 2(10) RPHA titre, the precipitin line corresponding to that of HBeAg/2-anti-HBeAg/2 was visualized in ID. Monoclonal anti-HBeAg antibody that absorbed only the precipitin line of HBeAg/1-anti-HBeAg/1 in ID was prepared for the characterization of HBeAg subtypes. A linear correlation (r = 0.91) between titres of HBeAg determined by the RPHA cells prepared with monoclonal and polyclonal antibodies was found in almost all HBeAg-positive sera. The reactivities of this monoclonal anti-HBeAg antibody to both HBeAg/1 and HBeAg/2 were demonstrated in affinity chromatography experiments using a Sepharose 4B column conjugated with this antibody. These results suggest that both HBeAg/1 and HBeAg/2 are constantly present in HBeAg-positive sera and that they are closely associated. Based upon these results, a hypothetical model for the elucidation of the immunological relationship between HBeAg/1 and HBeAg/2 is proposed.

Animals↗
PubMed1986

In-vitro antibacterial activity of BO-1165, a new monobactam antibiotic.

BO-1165 has excellent antibacterial activity against Gram-negative bacteria but it is almost inactive against Gram-positive and anaerobic bacteria. BO-1165 was more active than the four reference drugs against Escherichia coli, Salmonella spp., Shigella spp., Klebsiella pneumoniae, Serratia marcescens, indole-positive and indole-negative Proteus. Also, BO-1165 exhibited high antibacterial activity against strains of Pseudomonas aeruginosa (MIC50, 3.12 mg/l) and P. cepacia (MIC50, 1.56 mg/l), but did not against Ps. maltophilia strains. BO-1165 had good stability to plasmid-mediated and chromosome-mediated beta-lactamases. However, the compound was slightly hydrolyzed by the beta-lactamases isolated from Proteus vulgaris, Ps. cepacia, Klebsiella oxytoca and Ps. maltophilia, which were capable of hydrolyzing aztreonam.

Aztreonam↗