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Biomedical subjects

W Dobryszycka

Publications and source records attributed to W Dobryszycka.

At least 73 records · Page 4Linked to original sources

Serum enzymes in ovarian carcinoma.

The following enzymatic activities were measured in serum of patients with benign and malignant ovarian tumors before treatment: alkaline and acid phosphatases, aspartyl (AspAT) and alanyl (AlAT) aminotransferases, leucyl (LAP) and alanyl (AAP) aminopeptidases, lactate dehydrogenase (LDH), gamma-glutamyl transpeptidase, cathepsin, alkaline ribonuclease (RNase) and beta-glucuronidase. It was shown that at least three determinations (phosphatases and LAP) are practically useless in a discrimination between the examined groups. RNase in combination with AspAT (AlAT) or RNase with AAP and LDH were found to give the best results as marker enzymes.

Adenocarcinoma↗

Effect of modification on physico-chemical and biological properties of haptoglobin. Reaction with N-bromusuccinimide and 2-hydroxy-5-nitrobenzyl bromide.

N-Bromosuccinimide and 2-hydroxy-5-nitrobenzyl bromide have been used for modification of tryptophan residues in human haptoglobin (Hp) type 2-1. Modification of three exposed tryptophan residues reduced considerably both the Hp-haemoglobin interaction and binding of the antibody against the native protein. Modification of the remaining 7-8 tryptophan residues resulted in a complete loss of those properties. Antisera directed against Hp with the modified tryptophan residues appeared to be highly specific in immunological reactions.

2-Hydroxy-5-nitrobenzyl Bromide↗

Studies on the structure of haptoglobin and the haptoglobin-haemoglobin complex by spin and fluorescence labelling.

Human haptoglobin (Hp) of the 1-1 type incorporated one spin or fluorescence marker per molecule; the markers were found in the beta chain. Formation of the complex between spin-labelled Hp and haemoglobin or antibody caused conformational changes in the Hp molecular, evidenced by increased participation in the electron paramagnetic resonance spectrum of the component bound with the slowly rotating marker. From fluorescence-labelled Hp, the beta chain was isolated and cleaved by CNBr; only in one of the obtained peptides, one out of 4 histidine residues was modified with the marker.

Cyanogen Bromide↗

Blood serum peptidases in patients with ovarian carcinoma treated with Ledakrin.

The authors observed changes in activity of leucine amino-peptidase (E.C. 3.4.1.1--LAP), gamma-glutamyl transpeptidase (F.C 2.3.2.2--GGTP) and Co++-activated acylase in blood serum of patients with ovarian carcinoma, with or without ascites, treated with Ledakrin (1-nitro-9-[3-dimethylaminopropylamino] acridine). It was stated that the activities of LAP and GGTP increased during the treatment and during tumor progression. The level of Co++-activated acylase increased only slightly during the treatment and therefore, the determination of this enzyme appeared to be of no use in monitoring the therapy of ovarian carcinoma.

Acridines↗

Activities of some peptidases and glycolytic enzymes in cells of the amniotic fluid. i. Pregnancies terminated prematurely, at term, and postmaturely.

Activities of leucylaminopeptidase, gamma-glutamyl transpeptidase, oxytocinase and aldolase were significantly elevated in the cells of amniotic fluids from cases of premature delivery, compared with cases of delivery at term. The authors conclude that examination of the activities of the aforementioned enzymes can be utilized in prenatal diagnosis of the state of maturity of the fetus.

Amniotic Fluid↗

Influence of modifications of physicochemical and biological properties of haptoglobin. VII. Immunochemical reactivity of haptoglobin with modified tyrosine residues.

Tyrosine residues in human haptoglobin (Hp) type 2-1 were modified by treatment with various amounts of N-acetylimidazole, iodine or tetranitromethane. Rabbit antisera directed against native Hp, Ac-Hp, 1-Hp and NO2-Hp in cross-reactions by immunoprecipitation showed serologic identify of native Hp and most of the modified derivatives, with the exception of derivatives modified by means of a high excess of N-acetylimidazole, which showed partial identity with remaining preparations, irrespective of the antiserum used. The results indicate that tyrosine residues play no essential role in the immunochemical reactivity of haptoglobin.

Acetylation↗

Activities of some peptidases and glycolytic enzymes in cells of the amniotic fluid. II. Pregnancies complicated by threatening intrauterine fetal asphyxia.

Activities of leucylaminopeptidase, aspartyl aminopeptidase, gamma-glutamyl transpeptidase, oxytocinase, phosphohexoisomerase, phosphofructokinase and aldolase were studied in amniotic cells from cases of pregnancy complicated by threatening intrauterine fetal asphyxia. Leucylaminopeptidase and oxytocinase activities were much higher in the group of pregnancies complicated by threatening fetal asphyxia than in the control group. It was concluded that elevated activity of the aforementioned enzymes in cells of the amniotic fluid from pregnancies complicated by threatening intrauterine asphyxia is due to acute hypoxia of the fetus.

Adult↗

Biochemical studies on populations with long- or short-term exposure to environmental pollution.

Three groups of populations were studied: I. living for about 10 years, II. living for about 3 years near copper smelteries, and III. living in rural area, far from any source of air pollution. Lead content in blood was found to be 182.0 and copper 274.6 microgram/100 ml for group I, Pb - 69.2 and Cu - 253.3 microgram/100 ml for group II, and Pb - 43.8 and Cu - 143.3 microgram/100 ml for group III. Inhibition of glycolytic cycle enzymes and delta-aminolevulinic acid dehydratase was proportional to the duration of exposure to environmental pollution. Ceruloplasmin concentration in serum, as well as serum and red cells aminotransferases activities, were increased in group II and decreased in group I, suggesting certain mechanism of adaptation.

Air Pollutants↗

Cathepsins B1 from human fetal membranes.

Cathepsins B1 (EC 3.4.22.1) were isolated from fetal membranes of human placenta, i.e. amnion and chorion-decidua. Purification of the enzymes was achieved by the freezing-thawing technique, ammonium sulphate fractionation and Sephadex gel filtration. Cathepsis B1 separated either from amnion or from chorion-decidua exhibited optimum activity at pH 6.2, and an optimum temperature between 42-45 degrees C. They were inhibited by heavy metals, and compounds which react with the thiol groups. Isoelectric focusing demonstrated three isoenzymes of cathepsin B1 originating from chorion-decidua, while only one band was found for the enzyme from amnion.

Amnion↗

Preparation and properties of tRNA from human placenta.

1. The tRNA preparation obtained from human placenta by phenol extraction and DEAE-cellulose chromatography was homogeneous on ultracentrifugation and showed high amino acid acceptor activity. 2. The analysis of the isoaccepting tRNA by reversed-phase chromatography (RPC-5 system) showed the presence of 5 fractions for glycine and leucine, 3 for tyrosine, alanine and valine, 2 for arginine and 1 for phenylalanine.

Amino Acids↗

Effect of modification on physicochemical and biological properties of haptoglobin. VI. Reaction with azlactone of p-nitrobenzoyl-valine.

The azlactone of p-nitrobenzoyl-valine (Nbz-Val) has been used for modification of xi-amino groups of lysine in haptoglobin type 1-1, in hemoglobin, and in the haptoglobin-hemoglobin complex. By the use of this reagent 95% of amino groups in haptoglobin and 90% in hemoglobin have been blocked without any changes in peroxidase activity of the formed complexes: Nbz-Val.haptoglobin with hemoglobin, Nbz-Val. hemoglobin with haptoglobin, and Nbz-Val.(haptoglonin-hemoglobin). After reduction and reoxidation, Nbz-Val.haptoglobin was found to retain 90% of peroxidase activity when complexed with hemoglobin. Beta chains separated either from haptoglobin or Nbz-Val.haptoglobin showed 15% of peroxidase activity in the complex with hemoglobin, alpha chains of the same origin were completely inactive. Whereas recombination of haptoglobin from alpha and beta chains resulted in 42% hemoglobin-binding capacity, renaturation of Nbz-Val.haptoglobin from separated subunits was found to proceed with almost 100% yield. In immunodiffusion with rabbit anti-haptoglobin or anti-Nbz-Val.haptoglobin sera, preparations of haptoglobin and Nbz-Val.haptoglobin after reduction and reoxidation or after recombination from separated subunits gave similar precipitation arcs showing the reaction of immunological identity.

Haptoglobins↗

Effect of modification on physico-chemical and biological properties of haptoglobin. Acetylation, iodination and nitration.

Human haptoglobin (Hp) type 2-1 was modified with N-acetylimidazole, iodine or tetranitromethane (TNM), and the ability of the obtained derivatives to form with haemoglobin (Hb) complexes with peroxidase activity, was estimated. At low reagent to protein molar ratios, 11 tyrosine residues were nitrated, 12 acetylated and 13 iodinated. The biological activity of NO2-Hp and I-Hp amounted to 40% of the activity of native Hp whereas the activity of Ac-Hp only to 16%. The derivatives modified at high ratios of N-acetylimidazole or iodine lost the ability to bind with Hb. Deacylation. of tyrosines and partial liberation of acetylated xi-amino groups resulted in partial recovery of the activity. As demonstrated by polyacrylamide-gel electrophoresis, the modification of Hp with high excess of TNM or iodine induced polymer formation

Acetylation↗

Influence of industrial toxic compounds on pregnancy. VI. Some tissue enzymes in pregnant guinea pigs exposed to the action of triethylenetetramine.

Gamma-glutamyl transpeptidase activity in kidney homogenates, aspartate and alanine aminotransferase activities in liver homogenates, and cholinesterase activity in brain homogenates were determined in nonpregnant and pregnant guinea pigs exposed to absorption through the skin of the epoxy resin triethylenetetramine. Elevated activity of gamma-glutamyl transpeptidase in the kidneys of pregnant animals, and aspartate aminotransferase in the liver of nonpregnant guinea pigs were observed.

Acetylcholinesterase↗