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Biomedical subjects

M Warwas

Publications and source records attributed to M Warwas.

At least 19 recordsLinked to original sources
PubMed1989

Cathepsin H from human placenta.

Cathepsin H was isolated from human placenta by autolysis, acetone fractionation, and chromatography on DEAE-cellulose, Sephadex G-75, hydroxyapatite and concanavalin A-Sepharose. The enzyme gave on SDS-polyacrylamide gel electrophoresis two bands of Mr 25,500 and 28,500. Two active forms of the enzyme, with pI of 6.0 and 6.45, were obtained by isoelectric focusing. The enzyme is stable over the pH range 5-7.5, whereas it becomes inactive on heating to 50 degrees C. Cathepsin H of human placenta, like the enzyme from other sources, hydrolyses protein and naphthylamide substrates, showing within the latter group the strongest preference towards arginine-beta-naphthylamide (pH optimum 6.8). The enzyme is inhibited by the known inhibitors of cysteine proteases and by placental cystatins.

Cathepsin H↗
PubMed1989

Cystatins of human placenta.

Two low-molecular protein fractions inhibiting cysteine proteases were isolated from human placenta by alkalization to pH 11, acetone fractionation, affinity chromatography on CM-papain-Sepharose 4B, and Sephadex G-75 gel filtration. The results of polyacrylamide gel electrophoresis, isoelectric focusing indicate that one of there fractions in a dimer of cystatins B, and another is a mixture of cystatins A and B.

Cathepsin H↗
PubMed1987

[Cystatins].

Explore the source record for details and available documents.

Amino Acid Sequence↗
PubMed1986

Haptoglobin and proteinase inhibitors in the blood serum of women with inflammatory, benign and neoplastic lesions of the ovary.

Blood sera of women with myomas of the uterus, benign or malignant neoplasms of the ovary and with inflammatory conditions were examined by determining the haptoglobin concentration and functional activities of: alpha 2-macroglobulin, alpha 1-proteinase inhibitor and alpha-cysteine proteinase inhibitor. In the women with ovarian cancer, as compared with the control group, a significant increase of haptoglobin, alpha 1-proteinase inhibitor and alpha-cysteine proteinase inhibitor was found (p less than 0.001). On the contrary bioactivity of alpha 2-macroglobulin was depressed (p = 0.01). The observed increase of alpha-cysteine proteinase inhibitor activity in the groups with ovarian tumors and ovarian cysts was not related to the inflammatory state as estimated by the haptoglobin concentration.

Adult↗
PubMed1979

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↗
PubMed1977

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↗
PubMed1977

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↗
PubMed1977

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↗
PubMed1977

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↗
PubMed1976

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↗
PubMed1976

Evaluation of the influence of epoxide resins and their hardeners on the female body. II. Biochemical studies.

In women employed in an industrial plant in direct contact with epoxide resins and their hardeners, the following biochemical parameters were determined in blood: total protein, seromucoid, haptoglobin, hemoglobin variants, methemoglobin, alpha1-inhibitor of trypsin, lactate dehydrogenase, aspartate and alanine aminotransferases, alkaline and acid phosphatase, gamma-glutamyl transpeptidase, leucylaminopeptidase, and alanine aminopeptidase. Depending on duration of work, Hb A2 fraction and lactate dehydrogenase increased significantly, and aspartate aminotransferase, acid and alkaline phosphatase activities decreased. In pregnant women, leucylaminopeptidase activity and isozyme of placental alkaline phosphatase were decreased.

Acid Phosphatase↗