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Biomedical subjects

M Kondo

Publications and source records attributed to M Kondo.

At least 1,477 records · Page 82Linked to original sources
PubMed1976

Cold activation of complement i. presence of coagulation-related activator.

Determination of the complement titer in the serum and plasm of 120 patients with chronic liver diseases showed that in eight (7%) patients with cirrhosis of the liver, chronic active or chronic inactive hepatitis complement in the serum was less than half in the plasma. The dissociation of complement serum and plasma was due to cold activation of the classical pathway of complement in vitro since serum drawn from these patients at 37 degrees C lost hemolytic activity in 4 hours when transferred to a cold environment. Neither HB antigen nor cryoglobulin participated in this phenomenon. The activation of complement in the cold could be prevented by increasing the ionic strength, or by adding vitamin E or, to a lesser extent its vehicle HCO-60, while heparin, Trasylol, soybean trypsin inhibitor, or hirudin had no effect. Trans-AMCHA prevented activation in one case. It is speculated that a factor appearing as a result of blood clotting is able to activate the classical pathway of complement in the cold; it is probably not related to Hageman factor (factor XII), factor VII, thrombin, kallikrein.

Antithrombins↗
PubMed1975

Immune reaction in the gastric mucosa: passive mucosal anaphylaxis and experimental ulcer.

Immune reaction in the gastric mucosa using purified antigen-antibody system was investigated. Applying the technique of PCA on the gastric mucosa of dog, interesting phenomena named "Passive Mucosal Anaphylaxis (PMA) was obtained. The reaction could be produced even by the orally administered antigen. By the direct injection of soluble immune complex into the gastric mucosa, production of experimental ulcer was observed, in which parietal cells were relatively resistent to the immune tissue damage.

Anaphylaxis↗
PubMed1975

Synthesis and antitumor activity of 2-deamino- and N2-(gamma-hydroxypropyl)actinomycin D.

2-Deamino- and N2-(gamma-hydroxypropyl)actinomycin D were synthesized by modification of the parent actinomycin D molecule at the 2 position of the phenoxazinone moiety. The common intermediate was 2-deamino-2-chloroactinomycin D. Catalytic hydrogenation of this material afforded the 2-deamino derivative while treatment with gamma-hydroxypropylamine yielded the N2-(gamma-hydroxypropyl) derivative. These 2-substituted actinomycin D derivatives were less potent in microbiological assays than the parent compound. Evaluation of activity in vivo against three murine tumor systems indicated that optimal dose levels of 2-deaminoactinomydin D were 50 times greater than toxic dose levels of actinomycin D. N2-(gamma-hydroxyporpyl)actinomycin D exhibited antitumor activity similar to the parent compound.

1-Propanol↗
PubMed1975

Changes of ultrastructure in spore coat of Bacillus thiaminolyticus during germination and outgrowth.

Electron microscopic observation showed that the spore coat of Bacillus thiaminolyticus consisted of at least four layers; a high electron dense outer spore coat layer with five prominent ridges, a middle spore coat layer including two layers of a high and a low electron density, and an inner spore coat layer composing six to seven laminated layers. Rapid breakdown of the cortex and swelling of the core occurred in spores which were allowed to germinate by L-alanine for 45 min, whereas no change of surface feature was observed by scanning electron microscopy. Germination and outgrowth of spores in nutrient broth proceeded, being accompanied by morphological changes, in three steps; the first is a rapid breakdown of the cortex and swelling of the core, the second degradation of the inner layer at prominent region of the spore coat, and the last rupture of the spore coat and emergence of a young vegetative cell.

Bacillus↗
PubMed1975

Solubilization of coat protein from Bacillus thiaminolyticus spores.

Solubilization of spore coat protein of Bacillus thiaminolyticus was investigated using various reagents, and partial characterization of solubilized protein was carried out. Five per cent of the sodium dodecyl sulphate (SDS) treatment was the most effective for solubilization of coat protein, and 5% SDS + 8 M urea and 0.06 N NaOH were also useful. Acrylamide gel disc electrophoresis indicated that the SDS-soluble fraction mainly consists of a single band of protein and its molecular weight was estimated at about 15,000. The SDS+ urea-soluble fraction comprised two proteins with a molecular weight of 14,500 and 32,000, and an alkali-soluble fraction of 12,000 and 25,000 respectively.

Bacillus↗