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Biomedical subjects

J Kwiatkowska

Publications and source records attributed to J Kwiatkowska.

At least 19 recordsLinked to original sources
PubMed1991

[The mechanisms of insulin action].

Recent data on the mechanisms of insulin action are reviewed. The formation of second messengers from phosphatidylinositol-glycan precursor, and the influence of inositol-phosphate-glycan (IPG) on protein phosphorylation, and of diacylglycerol--on the gene expression is discussed.

Diglycerides↗
PubMed1985

Amelioration of hydroxyurea-induced suppression of phagocytosis in human granulocytes by free radical scavengers.

The exposure of human circulatory white cells in vitro to 0.1-1-10 mol/l hydroxyurea (HU) for 20 h induced a progressive dose-dependent suppression of the phagocytic activity of granulocytes. The suppressing effect of 20 h exposure to 1 mol/l HU was used to examine the protection afforded by free radical scavengers against HU-induced cytotoxicity. It has been found that, in the suitable concentration of the protecting agent, a substantial protective effect of sodium benzoate, acetylosalicylic acid, alpha-tocopherol, ascorbic acid, catalase, peroxidase or superoxide dismutase can be achieved.

Antioxidants↗
PubMed1985

Alkaline phosphatase from human uterine myoma. II. Kinetic and immunological properties.

Thermostability of the purified alkaline phosphatase derived from human uterine muscle and myoma was established before and after desialization. Both enzymes were inhibited by sucrose, glucose and maltose in proportion to the carbohydrate concentration. L-Homoarginine inhibits the myoma enzyme in 90%, L-leucine, L-histidine and L-tryptophan in about 60%, and L-phenylalanine in less than 15%. The type of inhibition and Ki values were determined. Muscle and myoma enzymes cross-reacted with antisera against human liver and placental isoenzymes. Molecular and kinetic properties of the enzyme were compared with known human isoenzymes of alkaline phosphatase.

Alkaline Phosphatase↗
PubMed1979

ATP-ase activity and lipid content of erythrocytes in treatment of acute lymphoblastic leukemia in children.

In erythrocytes of children with the acute lymphoblastic leukemia the rise in total phospholipid content, confined predominantly to lecithin, the decrease of cholesterol/phospholipid ratio and the increase of the Mg++-activated ATP-ase activity was found prior to treatment. The abnormalities of the lipid composition were in general persistent also in remission. The activity of erythrocytes ATP-ase decreased to normal values after achievement of the reversion of clinical and hematological symptoms of the disease. The increase of the enzyme activity may be induced by the in vitro incubation of normal erythrocyte with the blood plasma of patients in the acute stage of lymphoblastic leukemia but not in remission.

Adenosine Triphosphatases↗
PubMed1979

Modifications of erythrocyte phosphofructokinase in children with acute lymphoblastic leukemia. Acute stage and remission.

Erythrocyte phosphofructokinase from children with acute lymphoblastic leukemia was purified and characterized. In the acute stage of the disease the enzyme showed decrease affinity for substrate, reduced stability to heating and PCMB treatment, altered pH curve and increased effect of ATP as allosteric inhibitor. Only in one patient in remission, reversal of all enzyme abnormalities was found. In other cases, the general pattern of enzyme modifications was retained in spite of complete regression of clinical and hematologic symptoms. The only feature showing tendency to normalization in nearly all patients was the thermostability of phosphofructokinase. The results are discussed with regard to the mechanism of the enzyme's modification.

Adolescent↗
PubMed1979

Cobalt-activated acylase from human uterine myoma.

Cobalt-activated acylase was isolated from human uterine muscle and myoma. The enzyme was purified by ammonium sulphate precipitation, and subsequent chromatography on DEAE-cellulose, Sephadex G-150 and DEAE-Sephadex. The comparison of muscle acylase and acylase obtained from myoma has shown differences in the enzyme stability, the dependence of activity on pH and in the susceptibility to the effect of activators and inhibitors. Only one molecular form of cobalt-activated acylase has been found in both tissues.

Acyltransferases↗