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Biomedical subjects

W Kurzatkowski

Publications and source records attributed to W Kurzatkowski.

17 recordsLinked to original sources
PubMed1990

[Serum cathepsin A activity in pregnant, parturient and puerperal patients].

Cathepsin A activity has been determinal in sera of nonpregnant, pregnant (1st, 2nd and 3rd trimesto), puerperal (first, third and fifth day post partum) and parturient women in second stage (retroplacental blood and blood from umbilical cord) by means of N-Cbz-L-glutamyl-L-tyrosin after incubation with 37 degrees C and pH 5.5. There was an increasing cathepsin A activity with the duration of pregnancy, during labour and in the first puerperal days. Maximum of activity of cathepsin A has been determined in serum of retroplacental blood.

Carboxypeptidases↗
PubMed1990

[Physico-chemical studies of aluminum hydroxide in biological preparations preserved in different conditions].

An observation of physico-chemical properties of 0.5% Al(OH)3 and vaccines adsorbed to it (Di, Te, Di-Te, Di-Te-Per) stored for 3-24 months in various pH (5, 7, 8) and temperatures -18 degrees, +37 degrees, +45 degrees and +65 degrees was carried out. For this purpose an analysis of sedimentation rate, microscopic observation and ++roentgenographic analysis were performed. It was found that a decrease of storage temperature of Al(OH)3 gel and vaccines down to -18 degrees C resulted in some changes in structure and morphology of this absorbent (big precipitates) and it led to a significant increase of sedimentation rate.

Adjuvants, Immunologic↗
PubMed1989

[The activities of cathepsin A in the placenta, fetal membranes and amniotic fluid in physiologic pregnancy and pregnancy complicated by EPH gestosis].

Activity of cathepsin A was determined in placenta, fetal membranes and amniotic fluid as well in normal pregnancy as in complicated pregnancy by EPH-gestosis. Measurement of activity was done by N-CbZ-L-glutamyl-tyrosine with pH 5.5. Compared with normal pregnancy activity of cathepsin A was lower in the three materials of EPH-gestosis.

Amniotic Fluid↗
PubMed1987

Biosynthesis of benzylpenicillin by Penicillium chrysogenum and its Golgi apparatus.

The fine structure of high and low-yield mutants of Penicillium chrysogenum producing 10,000 and 100 units of benzylpenicillin was compared. The cells of both mutants showed typical eukaryotic ultrastructure. The Golgi vesicles, present in largest number in cells of high-yield mutant, fuse with the cell membrane and play an important role in the transport of benzylpenicillin from the cytoplasm to the cell environment. Benzylpenicillin was localized in cells of the high-yield mutant by means of enzymatical and immunological methods. The results indicate that benzylpenicillin is stored in the vesicles of the Golgi apparatus. The Golgi vesicles isolated from the protoplasts of high-yield mutant showed activities of enzymes of the pathway of benzylpenicillin biosynthesis i.e., delta-/L-alpha-aminoadipyl/-L-cysteinyl-D-valine synthetase, isopenicillin N synthetase, phenylacetyl: coenzyme A ligase, and acyl-exchange activity. Cell-free biosynthesis of antibiotic by the native Golgi vesicles was investigated in a well-defined reaction mixture. The native Golgi vesicles produced antibiotic in amount corresponding to 320 nmol.mg protein-1.h-1. The activity yield of the calcium alginate immobilized Golgi vesicles was 44%. Moreover, a hypothetical scheme for localization of the enzymes of pathway of benzylpenicillin biosynthesis in the cells of high-yield mutant is presented.

Acyltransferases↗
PubMed1985

Bacteriophages of Bacillus polymyxa.

Virulent bacteriophages of colistin--producing Bacillus polymyxa strains were studied. The phages were found to differ in lytic spectrum and were active only against strains of B. polymyxa. They did not attack other strains of the genus Bacillus. The virulent bacteriophages belong to two morphological groups differing in size. The size of the DNA of the bacteriophages of both groups is similar and ranges from 74.9 X 10(6) to 87.8 X 10(6) daltons. The cells of different B. polymyxa strains were also found to carry various defective phages which could be shown after mitomycin C induction of cell cultures. The antibacterial activity of mitomycin C induced cell lysates was not detected. Strains of B. polymyxa most probably devoid of defective bacteriophages (delysogenized) were isolated.

Bacillus↗
PubMed1979

The ultrastructure of Penicillium chrysogenum in the course of benzyl-penicillin biosynthesis.

The find structures of high- and low-yield mutants of Penicillium chrysogenum, producing 100 and 10,000 units/ml of penicillin G, were compared. The cells of both mutants demonstrated a typical eukaryotic ultrastructure. In the cytoplasm nuclei, mitochondira, lipid bodies, endoplasmic reticulum, and Golgi vesicles were observed. In the cells of high-yield mutant, during the biosynthesis of penicillin, the number of lipid bodies decreased. It is possible that the lipids are metabolized in the process of biosynthesis of penicillin. In the cytoplasm more multivesicular bodies and small vesicles, about 40 nm in diameter, could be seen. These Golgi vesicles, present in largest number in cells of high-yield mutant, fuse with the cell membrane and play an important role in the transport of penicillin from the cytoplasm to the cell environment. The cell walls of the high-yield mutant become three times thicker during the antibiotic biosynthesis. No comparable changes were observed in the ultrastructure of the low-yield mutant. The cell wall thickness did not increase, the cytoplasm contained few Golgi vesicles only, and the lipid bodies can be seen in all cells.

Cell Membrane↗
PubMed1979

The site of benzyl penicillin accumulation in Penicillium chrysogenum.

Benzyl penicillin was localized in cells of Penicillium chrysogenum by means of enzymatical and immunological methods, enabling the determination of minute amounts of penicillin. The reactions were performed on ultrathin sections. They allow to determine the antibiotic inside of the cells. The results indicate that benzyl penicillin is present in the vesicles belonging to the Golgi apparatus. Benzyl penicillin is transported from the cytoplasm outside the cell membrane by the Golgi vesicles.

Golgi Apparatus↗