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A Stankiewicz

Publications and source records attributed to A Stankiewicz.

At least 109 records · Page 6Linked to original sources
PubMed1982

[Erythrocyte zinc protoporphyrin concentration in occupational exposure to lead].

The paper is aimed at analysing the correlation between zinc protoporphyrin and hemoglobin concentrations and lead level in blood and the correlation between hemoglobin concentration and zinc protoporphyrin content in erythrocytes. The studies covered 73 men aged 19-58, exposed for 1-15 years. The control group was composed of 20 healthy men, age interval 17-66, with no occupational exposure to lead. A statistically significant difference for zinc protoporphyrin was demonstrated between the control and examined groups. No significant difference was found in hemoglobin concentration between those groups. On the other hand, a highly statistically significant increase with time was found in zinc protoporphyrin in erythrocytes. The dependence of zinc protoporphyrin concentration on lead concentration increases with employment length, reaching the correlation coefficient 0.6 after more than 9 years. No correlation was found between hemoglobin and lead concentrations in blood. Neither was it found between hemoglobin and zinc protoporphyrin concentrations.

Adult↗
PubMed1982

[Analysis of the statistical distribution of aminolevulinic acid dehydratase in a population not exposed to occupational chemical factors].

The subject of the paper has been to check the aminolevulinic dehydratase (ALAD) activity in those with no occupational exposure to inhibitors of this enzyme. Altogether 293 persons have been examined, 132 women and 161 men, aged 20-69. The resultant ALAD activity distribution showed no differences between women and men, though statistically significant differences have been found between the mean values. The distribution did not deviate from normal in both groups. The analysis of ALAD activity distribution in particular age groups, whether female or male, showed statistically significant differences. No clear dependence between ALAD activity and haemoglobin concentration in blood has been found. On the other hand, clear differences in ALAD activity between groups of high and low haemoglobin concentrations have been found. In addition to the mentioned examinations, 32 persons (12 women and 20 men) presently exposed to lead had their lead concentration determined in blood. No correlations have been found between lead concentrations in blood and ALAD activity.

Adult↗
PubMed1981

Deamination of adenosine 5'-phosphate and adenosine as a possible source of ammonia in human and bovine parotid glands.

1. The liberation of ammonia from adenosine 5'-phosphate (AMP) and adenosine and the release of inorganic phosphate from AMP were investigated in homogenates of bovine and human parotid glands. 2. Adenosine phosphate deaminase (AMP deaminase) was purified from bovine and human parotid glands. The enzyme preparations obtained were free from adenosine deaminase and 5'-nucleotidase activities. 3. AMP incubated with human parotid gland homogenate produced inosine 5'-phosphate, adenosine, inosine and ammonia. The amount of ammonia accumulating in the incubation mixture was equal to the sum of inosine 5'-phosphate plus inosine. 4. These results demonstrate the presence in human parotid of AMP deaminase and adenosine deaminase.

AMP Deaminase↗
PubMed1980

Isolation and regulatory properties of mitochondrial malic enzyme from rat skeletal muscle.

Mitochondrial malic enzyme (L-malate:NADP+ oxidoreductase (oxalo-acetate-decarboxylating), EC 1.1.1.40) has been isolated from rat skeletal muscle by (NH4)2SO4 fractionation, chromatography on DEAE-cellulose and Ultrogel AcA 34. Specific activity of the purified enzyme was 25 micromol/min per mg of protein which corresponds to about 840-folf purification. The enzyme was shown to carboxylate pyruvate in the presence of high concentrations of KHCO3 and pyruvate at about 15% of the rate of the forward reaction. The Km values determined at pH 7.2 for malate, NADP and Mn2+ were 0.33 mM, 6.8 microM and 7.1 microM, respectively. The Km values for pyruvate, NADPH and KHCO3 were 8.3 mM, 19.6 microM, and 24.4 mM, respectively. Purified enzyme showed allosteric properties at low concentration of malate and this characteristic can be modified by succinate and fumarate which do not affect the maximum velocity of the reaction. The pH optimum for decarboxylation reaction was between 7.2 and 8.4. Possible metabolic role of mitochondrial malic enzyme in skeletal muscle is discussed.

Animals↗