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Biomedical subjects

W Rzeczycki

Publications and source records attributed to W Rzeczycki.

15 recordsLinked to original sources

Effect of mesitylene on ethanol metabolism in rat liver microsomes.

Increased catalase activity was observed in the liver microsomal fraction of ethanol-treated rats (10% v/v aqueous ethanol solution per os for 5 weeks). In contrast, cytochrome P-450 concentration and specific activity of NADPH-cytochrome c reductase remained at the same level as in the liver of control rats (drinking water). The ratio of microsomal H2O2-generation to catalase activity was lower in the "ethanol" group than in the control one. This phenomenon seems to be related to the increased contribution of the "peroxidatic" reaction (increased rate of ethanol oxidation). Administration of mesitylene (1,3,5-trimethylbenzene) by gastric tube for 3 days (5 mmoles per kg daily) increased cytochrome P-450 concentration, specific activity of NADPH-cytochrome c reductase and ethanol metabolism.

Alcoholism

Collagen-bound glycoprotein of Guerin epithelioma.

The polymeric collagen of Guerin epithelioma is strongly bound to a large amount of noncollagenous substance. Almost full dissociation of this complex was achieved by heating in 7 Murea, at 100 degrees C for 4 hours. The collagen bound substance was identified as an acidic glycoprotein containing glucose, galactose, glucosamine, galactosamine and M-acetylneuraminic acid. Heterogeneity of this substance in regard to molecular weight was found.

Amino Acids

Characterization of cytoplasmic arginine-rich basic protein of Guerin epithelioma.

Arginine-rich basic protein from cytoplasma of Guerin epitheliomas has been isolated and characterized. It contains five amino acids: arginine, lysine, glycine, alanine and glutamic acid which make together 74% of all amino acid residues. The protein has a cationic character with an isoelectric point of 8.2. No carbohydrate component was found in this protein. The significance of arginine-rich basic protein in the cytoplasma of Guerin epithelioma is discussed briefly.

Amino Acids

Participation of thyroid D-aspartate oxidase in iodide oxidation and incorporation into thyroid proteins.

It was found that the H2O2 generating system containing D-aspartate oxidase isolated from the thyroid gland and D-aspartate, takes part in oxidation of iodides. The molecular I2 formed under experimental conditions is subsequently incorporated into thyroid proteins. Thiosemicarbazide, thiourea, methylthiouracyl, sulphathiazole, thiocyanate and azides were found to have an inhibiting effect on iodide oxidation. Methimazole inhibits both the oxidation of iodide and incorporation of 131I into protein. The iodide incorporation was inhibited by catalase. The findings of these investigations suggest an indirect participation of D-aspartate oxidase in the synthesis of the thyroid hormone by supplying the essential substrate for the iodide oxidation, H2O2.

Amino Acid Oxidoreductases

The comparison of aminotransferase activities in normal and Guerin epithelioma bearing rats.

The activities of 13 aminotransferawes in Guerin epithelioma and in the liver of normal and tumor bearing rats were investigated. Alanine and aspartate aminotransferases show the highest activity in all investigated tissues. In the liver of normal rats high arginine, tyrosine and phenylalanine aminotransferase activities were found. In tumor tissue high level of branched chain amino acid (leucine, valine and isoleucine) aminotransferases were observed. Increase in aminotransferase activities in the liver of tumor bearing rats was found. In order to elucidate the mechanism of this increase an inductive effect of hydrocortisone and protein free extract of tumor tissue on liver aminotransferases has been investigated. The tumor extract did not exert an inductive action. An inductive effect of hydrocortisone was not identical with the change in aminotransferase activities observed in the liver of tumor bearing rats.

Alanine Transaminase

Insoluble collagen of methylcholanthrene induced sarcoma.

The insoluble collagen from methylcholanthrene induced sarcoma was isolated and characterized. It contains more glycine, hydroxyproline and acidic amino acids than normal connective tissue collagen. An anionic character of tumour collagen was stated (pI 6.1). No typical collagen subunits in this protein were found. The tumour collagen is strongly bound to acidic glycoprotein containing a significant amount of hydroxylysine. Such an insoluble complex is resistant to the dispersing action of EDTA. It dissociates during heating in concentrated urea.

Adenine

Isolation, purification and chemical composition of insoluble collagen from Guerin epithelioma.

1. The insoluble collagen from Guerin epithelioma was isolated and its chemical composition was determined. The unusually high histidine content is accompanied in tumour collagen by a relatively small amount of lysine and arginine. 2. The isolated protein was strongly bound to glycoprotein, which could not be removed by EDTA treatment unless this procedure was preceded by digestion of the complex with trypsin.

Animals