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Biomedical subjects

H Urbanek

Publications and source records attributed to H Urbanek.

14 recordsLinked to original sources
PubMed2005

Induction of glutathione S-transferase and glutathione by toxic compounds and elicitors in reed canary grass.

Treatment of read canary grass leaves with phenol, 4-chlorophenol, naphthalic anhydride and phenylethylisothiocyanate increased glutathione S-transferase activity by 1.4-2.4-fold (control 17 U g(-1) DW). Benzothiadiazole, beta-aminobutyric acid and salicylic acid increased activity by 1.3-1.8-fold. Total glutathione pool was increased by the toxic compounds by 1.2-2-fold and by the elicitors 1.4-1.6-fold (control 593 nmol g(-1) DW). Unlike the other compounds, benzothiadiazole and salicylic acid did not decrease the redox state. Benzothiadiazole acted synergistically with chlorophenol on glutathione S-transferase and glutathione levels and counteracted the decrease in redox state caused by the xenobiotic. Reed canary grass thus has a strong potential to neutralize toxic compounds, which may be further enhanced by elicitors.

Aminobutyrates↗
PubMed1998

[Pseudo-abnormal venous lung blood flow in trained endurance athletes].

Pulmonary venous flow was recorded by transthoracic pulsed Doppler echocardiography in 10 endurance trained male athletes and in 10 age matched sedentary male controls. The ratio of peak systolic (S) to peak diastolic (D) flow velocity was much lower in athletes than in controls (0.8 +/- 0.22 vs. 1.13 +/- 0.37 p < 0.05). 5 out of 10 athletes had values less than 0.82 which was the lowest value in the control group. Athletes also hat significantly higher mitral flow E/A ratios and lower heart rates. Physical fitness caused by endurance training should be acknowledged one of the causes for an abnormally low S/D ratio.

Adult↗
PubMed1996

Generation of superoxide anion and induction of superoxide dismutase and peroxidase in bean leaves infected with pathogenic fungi.

Generation of superoxide anion (O2-.) and peroxidase activity were significantly increased in bean leaves infected with incompatible and compatible pathogens: Botrytis fabae and Botrytis cinerea, respectively, but the induction was greater on direct inoculation with B. fabae, than with B. cinerea. A slightly higher O2-. level was also detected in the parts of leaves surrounding the inoculation side. Overproduction of O2-. was observed earlier than the increase in peroxidase activity. Pretreatment of the leaves with methyl jasmonate enhanced both O2-. production and peroxidase activity following inoculation with B. cinerea. Induction of superoxide dismutase activity after the infection was less pronounced than changes in O2-. level. The differences in the rate of NADH oxidation in the extracts from control and inoculated leaves, correlated with the differences in the rate of O2-. production. The results indicate that O2-. level is one of the essential factors responsible for the difference in the interactions between bean plant and compatible and incompatible pathogens.

Fabaceae↗
PubMed1990

Changes in peroxidase activity in cell structures of lupin roots infected by Fusarium culmorum.

Infection of lupin seedlings with Fusarium culmorum results in the increase in peroxidase activity with syringaldazine as a substrate, mostly in microsomes and cell walls, in the latter fraction somewhat later than in microsomes and cytosol. Less evident were the changes upon infection in peroxidase activity with guaiacol as a substrate. Both qualitative and quantitative differences in the peroxidase forms were evidenced on electrofocusing of the enzyme in the examined subcellular fractions.

Cell Wall↗
PubMed1988

[Diabetic angiopathy and surgical consequences as a basis for rehabilitation].

Diabetes mellitus is a major risk factor for the development of arterial occlusive disease. 2 kinds of diabetic angiopathy with different sequelae can be found needing surgical therapy after failure of conservative treatment; quite often it is necessary to perform an amputation sooner or later. By sufficient walking exercises and exact preoperative workup it is possible to find a favourable level of amputation. Good operative technique and early postoperative mobilisation of the patient can lead to complete rehabilitation.

Amputation, Surgical↗
PubMed1985

Extracellular proteinases of the isolate of Botrytis cinerea virulent to apple tissues.

B. cinerea produces extracellular acid proteinases: aspartic proteinase and carboxypeptidase, separable on CM-Sepharose CL-6B. Aspartic proteinase showed the maximum activity at pH 2.5-3.0, was inactivated by diazoacetyl-DL-norleucine methyl ester and was unable to hydrolyse carbobenzoxy Glu-Tyr. Carboxypeptidase showed the maximum activity at pH 4.7-5.0, was inactivated by diisopropyl fluorophosphate, and carbobenzoxy-Glu-Tyr served as an efficient enzyme substrate. The isolated aspartic proteinase hydrolysed proteins in the preparations of apple cell walls. Excretion of aspartic proteinase by B. cinerea preceded that of carboxypeptidase.

Carboxypeptidases↗
PubMed1984

Hydrolytic ability of acid protease of Fusarium culmorum and its possible role in phytopathogenesis.

It was found that the acid protease of Fusarium culmorum can hydrolyze various proteins of plant origin including polygalacturonase inhibitor from bean (BPI) and soybean trypsin inhibitor (STI). The highest hydrolysis extent of BPI and STI by the enzyme was only 5% and 3% respectively. The partially hydrolyzed BPI lost its inhibition ability to fungal polyglacturonases. Similarly, the partially hydrolyzed STI lost its inhibition ability to trypsin and fungal alkaline protease. The F. culmorum acid protease showed broad substrate specificity towards synthetic dipeptides.

Amino Acid Sequence↗
PubMed1975

Polygalacturonase of Botrytis cinerea E-200 Pers.

A polygalacturonase (poly(1,4-alpha-D-galacturonide)glycanohydrolase, EC 3.2.1.15) was purified from the culture fluid of Botrytis cinerea. The polygalacturonase preparation, homogeneous on the basis of disc-gel electrophoresis also showed pectinesterase activity. Some properties of the purified polygalacturonase were studied. It had a molecular weight about 69 000. It was inactivated by p-chloromercuribenzoate, tetranitromethane and urea. A 50% loss in viscosity of sodium polypectate solution occurred when 4.6% of the glycosidic bonds were hydrolyzed. The only end product of sodium polypectate and oligogalacturonides hydrolysis was monogalacturonic acid.?

Chloromercuribenzoates↗
PubMed1975

Isolation and Some Properties of Glucoamylase from Cephalosporium charticola Lindau.

High glucoamylase (alpha-D-/1 --> 4/glucan glucohydrolase, EC 3.2.1.3.) activity was obtained in the cell-free culture fluid of Cephalosporium charticola. Glucoamylase seems to be the only amylolytic enzyme produced by C. charticola. The enzyme, purified on diethylaminoethyl-cellulose, was homogeneous by disc gel electrophoresis. The optimum pH on starch was 5.4, and optimum temperature was 60 C. Starch was degraded more rapidly than several other substrates; maltose was hydrolyzed about one-fifth as rapidly as starch. The molecular weight was 69,000, as determined by Sephadex G-100 filtration. The enzyme is a glycoprotein and contains about 6.6% sugars (mannose and glucosamine).

Journal Article↗