PubMed Health⌕ Search

Biomedical subjects

J W Naskalski

Publications and source records attributed to J W Naskalski.

17 recordsLinked to original sources
PubMed1990

[Proteinuria].

Explore the source record for details and available documents.

Diagnosis, Differential↗
PubMed1989

Determination of ribonuclease activity in serum of patients with pancreatic necrosis. An attempt of extending the enzyme diagnosis of acute pancreatitis.

Though the substantial part of serum ribonuclease (EC 3.1.27.5) is of pancreatic origin, there are no consistent data on changes in activity of serum alkaline ribonuclease in acute pancreatitis. The recent findings suggest that the increase in ribonuclease activity refers only to patients with necrotic outcome of acute pancreatitis. The aim of this study was to reevaluate the suggestion that elevated ribonuclease activity is specifically related to pancreatic necrosis. Our studies included 57 patients with verified acute pancreatitis, and 11 patients evolving haemorrhagic or necrotic lesions of the pancreas. It was found, that the enzyme increasing in some percentage of patients with acute pancreatitis is the Poly-C avid "pancreatic" ribonuclease. This enzyme begins to increase in the 2nd or third day after onset of the disease, always after decrease in serum amylase activity down to levels close to normal range. Ribonuclease activity increased up to days 5 or 6 of the disease, and then decreased along with diminution of disease symptoms upon treatment. Correlation studies showed that increased ribonuclease activity in acute pancreatitis is related to a higher than the 2nd degree of severity of the clinical course of the disease, to pancreatic necrosis, death, diminished glomerular filtration rate, and age. Thus, pancreatic necrosis is not the exclusive factor directing the increased ribonuclease activity in acute pancreatitis, but the increased ribonuclease activity seems to be a late marker of acute pancreatitis of a severe clinical course.

Acute Disease↗
PubMed1988

Oxidation of amino acids and peptides in reaction with myeloperoxidase, chloride and hydrogen peroxide.

Oxidation was studied of N-acetyl derivatives of cystine, cysteine, methionine and glycyltryptophan employing the myeloperoxidase-Cl--H2O2 system at pH 4.5, 6.0 and 7.0. Moreover, oxidation of pentapeptide composed of Leu-Trp-Met-Arg-Phe-COOH with myeloperoxidase (donor:hydrogen-peroxide oxidoreductase, EC 1.11.1.7) and hypochlorite was also studied. It was found that amino-acid derivatives having an amino group bound to an acetyl residue react with functional groups of the side-chain. The -SH groups of N-acetylcysteine and the -SS- group of cystine oxidize to cysteic acid. Methionine residues oxidize to methionine sulphoxide, and tryptophan residues to a derivative of 2-oxoindolone. The same reaction products were obtained when respective amounts of hypochlorous acid were used instead of myeloperoxidase, Cl- and H2O2. Differences in the stoichiometry of reactions of myeloperoxidase-mediated oxidation and hypochlorite oxidation suggest differences in the reaction mechanisms of both studied systems. Interaction of the studied pentapeptide with myeloperoxidase-Cl(-)-H2O2 system as well as with hypochlorite showed that in the peptide molecule individual amino acids oxidize consecutively according to their susceptibility to oxidation. No splitting of peptide bonds was observed. Therefore, a modified peptide with methionine sulphoxide and and oxidized tryptophan incorporated into the molecule was obtained.

Amino Acids↗
PubMed1988

Lysozyme oligomers as a molecular mass standard for sodium dodecyl sulfate-polyacrylamide gel electrophoresis.

Egg white lysozyme treated with hypochlorous acid links together producing di-, tri-, tetra-, and pentameric derivatives with molecular masses ranging from 14,300 to 90,500. Similar oligomeric products may be obtained by treating lysozyme color derivatives produced by labeling lysozyme with fluorescein, trinitrobenzenesulfonic acid and 2,4-dinitrofluorobenzene, with hypochlorous acid. The oligomeric lysozyme derivatives thus obtained consist of a mixture of proteins with molecular masses equal to multiples of 14,300 (lysozyme molecular mass). This mixture can be applied as a set of molecular mass standards suitable for determination of protein molecular masses on sodium dodecyl sulfate-polyacrylamide gel electrophoresis.

Electrophoresis, Polyacrylamide Gel↗
PubMed1988

Action of myeloperoxidase-hydrogen peroxide-chloride system on the egg white lysozyme.

The enzyme system composed of human neutrophilic myeloperoxidase (H2O2-oxidoreductase, EC 1.11.1.7), H2O2 and Cl-, at pH 4.5 interacts with egg white lysozyme (EC 3.2.1.17) in several stages. In the first stage, occurring at lysozyme to H2O2 molar ratio of 1:1.4-1.8, the lysozyme loses its enzyme activity but does not yield any derivative distinguishable from the native protein on polyacrylamide gel electrophoresis (PAGE). The second stage of oxidation begins at lysozyme to H2O2 molar ratio above 1:5, producing a change in the lysozyme spectrum at 260-290 nm, and yielding protein derivatives with molecular masses equal to multiples of 14.3 kDa, i.e. the lysozyme molecular mass. This implies that an excessive oxidation of lysozyme by the myeloperoxidase-H2O2-Cl- system produces cross-linking of lysozyme molecules to di-, tri-, tetra-, and pentameric structures. At lysozyme to H2O2 molar ratio exceeding 1:12 a water insoluble white product, which consists of a set of lysozyme cross-linked derivatives, is obtained.

Acetylcysteine↗
PubMed1987

Proteinuria and excretion of ribonuclease in patients with chronic granulocytic leukaemia.

Elevated RNase activity which occurs in serum and urine of CGL patients parallels the urinary protein excretion. Acid RNase and alkaline RNase activities in urine of CGL patients, as well as acid and alkaline RNase clearance values correlated with the urinary protein concentration. Mean urinary protein level in CGL patients was approximately twice as high as that in controls. The molecular mass of CGL urinary proteins ranged from 12,000 to 80,000 proving the LMWP type of proteinuria. No particular protein contributed to the elevation of LMWPs in CGL urine. Among numerous protein fractions, albumin, acid alpha 1 glycoprotein, prealbumin RNase and in a few cases LZM were observed. The results of this study suggest that the increase of RNase activity in serum and urine reflects a more general phenomenon of increase in excretion of the entire set of LMWPs.

Adult↗
PubMed1986

Ribonuclease from cytosolic fraction of human erythrocytes.

Ribonuclease (RNase) activity is detectable in only one third of specimens of human erythrocyte haemolysates. On the other hand, treatment of erythrocytic cytosoles with sulphosalicylic acid reveals an inhibitor-bound RNase activity which is present in all erythrocyte specimens studied. The level of the erythrocyte inhibitor-bound RNase activity is comparable to that in human lymphocytes. Isolated RNase from the cytosolic fraction of human erythrocytes is poly-C avid RNase with maximum activity at pH 6.5. The enzyme is resistant to treatment with strong acids and heating up to 95 degrees C. Molecular filtration of the erythrocyte RNase shows that it is composed of two fractions differing in molecular mass, 19 000 and 15 000. No difference in enzymic properties between these fractions was found. The general properties of erythrocyte cytosolic RNase are much like those of acid RNases of human granulocytes and lymphocytes. As the erythrocytes do not metabolize RNA no function for the inhibitor-bound RNase can be suggested. Assuming that the observed erythrocyte RNase is the residual enzyme, persisting in the cell since it was functioning in the nucleated erythrocyte precursors, one may surmise that levels of free and inhibitor-bound erythrocyte RNase activity may be related to the normality or abnormality of erythrocyte maturation.

Adolescent↗
PubMed1986

Cyclic 3':5'-adenosine monophosphate phosphodiesterase and cyclic 3':5'-guanosine monophosphate phosphodiesterase of normal granulocytes and granulocytes of chronic myelogenous leukaemia.

Normal human neutrophilic granulocytes and granulocytes of chronic myelogenous leukaemia (CML) were shown to possess only the "high Km type" isoenzyme of cAMP-phosphodiesterase. The properties of this enzyme are similar in both normal and CML granulocytes. cGMP-phosphodiesterase in human granulocytes was found to be composed of "high Km type" and "low Km type" isoenzymes. The high Km cGMP-phosphodiesterase of CML granulocytes showed a considerably lower apparent Km and Vm value than those in normal neutrophilic granulocytes.

3',5'-Cyclic-AMP Phosphodiesterases↗
PubMed1986

Correlation of granulocyte intracellular activities of cyclic nucleotide phosphodiesterases with leukocyte count in patients with chronic myelogenous leukaemia.

The activity of adenosine cyclic 3':5'-monophosphate phosphodiesterase in granulocytes of patients with CML essentially depends on the granulocyte donor's WBC count. The ratio of cAMP-PDE/cGMP-PDE activities in CML granulocytes strongly correlates with CML host WBC count. The regression analysis of cyclic nucleotide phosphodiesterase activities and counts of individual constituents of the white blood cell population present in the blood of CML patients showed the primary relationship between the natural logarithm of total WBC count and the cAMP-PDE/cGMP-PDE activity. The results suggest that the properties of CML granulocytes depend on the accumulation of these cells in the CML host.

3',5'-Cyclic-AMP Phosphodiesterases↗
PubMed1985

Activity of cyclic nucleotide phosphodiesterases in granulocytes of chronic myelogenous leukemia (CML). A preliminary report.

Cyclic 3':5'-adenosinmonophosphate phosphodiesterase (cAMP-PDE), high KM value type isoenzyme, and cyclic 3':5'-guanosino-monophosphate phosphodiesterase (cGMP-PDE), high KM value type isoenzyme, were determined in granulocytes of patients with chronic myelogenous leukemia (CML) in the chronic phase of the disease. Granulocyte cAMP-PDE activity was similar in the general group of CML patients to that in normal granulocytes; the cGMP-PDE, however, was somewhat higher. By dividing the CML general group into the "low leukocyte count" subgroup including granulocytes of patients with WBC number ranging from 10,300 to 40,000 per microliter (mean 22,000 per microliter), and the "high leukocyte count" subgroup including patients with leukocyte count above 40,000 per microliter (mean 67,000) remarkable differences in the activities of cyclic nucleotide phosphodiesterases between these subgroups could be found: cAMP-PDE activity for the high leukocyte count subgroups was significantly higher than for that in normals, and in CML-low leukocyte count subgroup. On the other hand, cGMP-PDE activity in granulocytes of the high leukocyte count subgroup was found to be remarkably lower than that in normals, in the low leukocyte count subgroup and general CML group. In CML patients the ratio of cAMP-PDE activity to cGMP-PDE activity was always considerably higher than that in controls. The obtained results suggest CML granulocytes to differ from normal ones in respect to their control of intracellular cyclic nucleotide levels. This difference is related to the accumulation of CML granulocytes.

3',5'-Cyclic-AMP Phosphodiesterases↗
PubMed1979

Elevation of an acid ribonuclease in serum of patients with chronic granulocytic leukaemia.

Ribonuclease (Ribonucleate nucleotide 2'-transferase E.C. 2.7.7.17) activity in serum of patients with chronic granulocytic leukaemia measured at pH 4.5-6.0 amounts to more than three times of that in serum of healthy subjects. At pH 6.0-8.0 the elevation of ribonuclease activity in serum of patients with chronic granulocytic leukaemia is less pronounced and amounts to about two times of that in normal ones. Using chromatography on CM Sephadex C-50 column, serum ribonuclease of both normal and chronic granulocytic leukaemia patients was separated into five distinct fractions. In serum of healthy subjects ribonuclease fractions denoted I-V contribute to 10; 21; 29; 22, and 18 percent of the total ribonuclease activity. In the serum of patients with chronic granulocytic leukaemia a decrease in ribonuclease fraction III to merely 17 percent and an increase in contribution of fraction IV to 32 percent of total ribonuclease activity could be observed. The comparison of each individual concentration of fraction in normal and leukaemia patients serum reveals, that ribonuclease fraction IV will increase about 3 times. A less pronounced increase could also be found for fractions I, II and V. However, ribonuclease fraction IV may be supposed to carry more than 50 percent of the whole extra load of ribonuclease present in the serum of chronic granulocytic leukaemia patients.

Acids↗
PubMed1977

Myeloperoxidase inactivation in the course of catalysis of chlorination of taurine.

Myeloperoxidase (donor: hydrogen-peroxide oxidoreductase, EC 1.11.1.7) was isolated from leukocytes of patients with chronic granulocyte leukemia. In the presence of H2O2 and Cl- at pH 4.0-6.6 the myeloperoxidase catalyses chlorination of taurine to monochloramine taurine and simultaneously undergoes inactivation. The myeloperoxidase inactivation rate depends on the concentration of H2O2 and Cl-: both the initial rate of chlorination and myeloperoxidase inactivation rate increase with increasing concentration of H2O2. However, an increase in concentration of Cl- results in a decrease in enzyme inactivation. At a given H2O2 concentration, myeloperoxidase inactivation is a first order reaction, which implied that the enzyme may react with a substrate a limited number of times.

Chlorides↗
PubMedDate not supplied

Determining of actual activities of acid and alkaline ribonuclease in human serum and urine.

Acid and alkaline ribonuclease (RNase) activities were measured in serum and urine using procedure based on assumption that all determined RNase activities, both at pH 6.5 and 7.8 represent values produced by overlapping of activities of acid leukocyte type RNase and alkaline pancreatic type RNase. The procedure requires simultaneous determining of RNase activity at pH 6.5 and 7.8 and further calculation of actual activities of acid and alkaline RNase activities using the elaborated experimental formula. Results of determining acid and alkaline RNases in human sera yielded on information on specific contribution of leukocyte type and pancreatic type RNases to increased RNase activity in such clinical conditions as terminal renal failure, myocardial infarction and chronic myelogenous leukemia. It was also found that there is in human urine a remarkably increased proportion of acid RNase activity if compared to this in serum.

Humans↗