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Biomedical subjects

W Matuszewski

Publications and source records attributed to W Matuszewski.

At least 37 records · Page 2Linked to original sources
PubMed1976

[The vehaviour of monoaminooxydase (MAO) activity in tumours. I. MAO activity measurement in experimental tumours (author's transl)].

The activity of MAO (EC 1.4.3.4) was measured in liver homogenates of mice with experimental tumours Sarcoma S-180 and Leukemia L-1210. The enzyme activity was determined by two methods: spectrophotometric--with benzylamine as a substrate and the second with the application of oxygen electrode and adrenaline as a substrate. An increase of the enzyme activity was observed in liver homogenates of mice with Sarcoma S-180 as compared with the controls. High activity of MAO with both substrates was also observed in Sarcoma ascites. In Leukemia L-1210 changes of activity in relation to adrenaline as a substrate were very small, but towards benzylamine the affinity of enzyme was higher (the increase of activity was about 50%).

Animals↗
PubMed1975

Changes of certain pharmacological and biochemical indices in acute methylglyoxal poisoning.

Methylglyoxal in doses over 25 mg/kg injected intravenously in cats and rabbits produces distinct changes in the cardiovascular and respiratory systems, but has no effect on respiration or circulation when injected intraperitoneally even in doses up to 1 g/kg. The effect of MG on blood pressure depends on the species of the animal. The effects of MG are dose-related and dependent on the route of its administration. Biochemical studies showed a significant rise in serum activities of creatine kinase (EC 2-7-3-2), lactate dehydrogenase (EC 1-1-1-27) and aspartate aminotransferase (EC 2-6-1-1-) after intraperitoneal injection of MG in the dose of 200 mg/kg in rabbits and 500 mg/kg in rats. The observed changes probably indicate damage of muscle tissue by MG, presumably as a result of low content of one of the glyoxalases in the muscles of the experimental animals. Elevation of glucose levels by MG was probably an adrenergic effect. These biochemical changes can serve to evaluate toxicity of MG preparations, which exhibit variations probably owing to varying degree of polymerization.

Alanine Transaminase↗
PubMed1973

gamma,delta-Dioxovalerate as a substrate for the glyoxalase enzyme system.

1. Crude gammadelta-dioxovalerate was synthesized from laevulinate by two different methods and was purified by Sephadex chromatography. Some analytical reactions of the compound are described. 2. gammadelta-Dioxovalerate is a substrate for glyoxalase I and the GSH derivative formed by this enzyme is hydrolysed by glyoxalase II to form d-alpha-hydroxyglutarate. The K(m) of glyoxalase I for gammadelta-dioxovalerate is 1.0x10(-3)m at pH5.8.3. The u.v.-absorption spectrum of thiol ester, synthesized enzymically from gammadelta-dioxovalerate and GSH by glyoxalase I, is almost identical with that for S-lactoylglutathione. Some optical properties of this thiol ester were measured. 4. Attempts to show reversibility of the glyoxalase system reactions with d-alpha-hydroxyglutarate as substrate were unsuccessful. 5. The possible metabolic role of the gammadelta-dioxovalerate reaction is discussed. It is suggested that one of the metabolic functions of the glyoxalase system may be to provide a mechanism for the entry of this compound into the tricarboxylic acid cycle.

Aldehydes↗