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A Stankiewicz

Publications and source records attributed to A Stankiewicz.

At least 91 records · Page 5Linked to original sources
PubMed1984

[Erythrocyte protoporphyrin IX in occupational exposure to asbestos].

Analysis of the dependence of protoporphyrin IX in erythrocytes upon non-exposed populations age. The study was performed in 246 persons (104 women and 142 men) who were not occupationally exposed to toxic agents. The women were aged 19-72, the men 19-76. The mean concentrations of protoporphyrin IX for those groups do not differ significantly. To test the dependence of protoporphyrin IX concentration upon age, the women and men were divided into three age subgroups: under 30, 31-40, and over 40. The statistical analysis indicated different distribution of mean protoporphyrin IX concentrations at those age intervals in both test groups, no significant difference between those values being found. Effects of asbestos upon protoporphyrin IX concentrations in erythrocytes in occupational exposure. Sixty three persons were examined (27 women and 36 men), workers of the Plant of Asbestos Seals and Products, "POLONIT", Lódź. The exposure lasted 1-35 years. Age intervals: women 25-64, men 25-63. The estimated mean protoporphyrin IX concentrations both for women (51.2 mg%) and men (47.6 mg%) differ significantly from the mean values of relevant control groups (39.3 and 37.6). In addition, ferrum concentration in serum and hemoglobin concentration in blood in the mentioned groups were analysed. All the findings were within the physiological values.

Adult↗
PubMed1983

High substrate affinity and GTP insensitive AMP deaminase from frog liver.

1. Relatively high activity of AMP deaminase (2.5 mumol/min/g wet wt of tissue) estimated at 70 microM AMP concentration was found in frog liver. 2. The enzyme was purified to homogeneity, its subunit and native protein molecular weights were about 70,000 and 330,000 respectively. The specific activity of the purified enzyme was 44 mumol/min/mg of protein at 70 microM AMP and Km for AMP was 0.7 mM. 3. The enzyme was rather specific for AMP, several structural analogues of 5'AMP were deaminated at the rate not exceeding 5% of the rate of AMP deamination. 4. Frog liver AMP deaminase was activated by monovalent cations, highest rate of reaction was observed in the presence of potassium, rhubidium and sodium ions. The enzyme was activated by ADP and ATP and inhibited by inorganic phosphate but was not influenced by GTP.

AMP Deaminase↗