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K Kotelko

Publications and source records attributed to K Kotelko.

18 recordsLinked to original sources
PubMed1983

Some biological features of Proteus bacilli. 1. Comparison of Proteus mirabilis strains provided from various sources.

Some properties which may contribute to the pathogenicity of Proteus mirabilis were compared in urinary isolates and in strains provided from soil and from culture collection. Clinical isolates revealed the higher expression of all the features examined in this report: swarming growth, haemagglutination, adherence to human uroepithelial cells, urease activity and haemolytic activity. Noteworthy is the higher mean value of adherence to the uroepithelial cells in clinical strains. Three P. mirabilis urinary isolates were detected which produce an as yet unreported filterable haemolysin. However, the loss of this ability within a few months seems to suggest the temporary presence of a plasmid rapidly eliminated by the Proteus strains.

Adhesiveness↗
PubMed1983

Some biological features of Proteus bacilli. 2. Haemolytic activities of Proteus mirabilis and Proteus vulgaris strains.

The haemolytic activities of Proteus mirabilis and P. vulgaris strains were studied under different conditions. No filterable alpha haemolysin could be detected in P. mirabilis uropathogens provided from patients with urinary tract infections. Together with the results presented in the accompanying paper, in which three clinical isolates with temporary ability to produce a soluble haemolysin were described, the occurrence of alpha haemolytic P. mirabilis isolates did not exceed 3%. Cell bound beta haemolysin is present in nearly 35% of P. mirabilis urinary strains. Another kind of haemolytic activity was observed when P. mirabilis and P. vulgaris strains were grown in liquid media supplemented with erythrocytes. During the logarithmic growth phase nearly 100% of P. mirabilis and P. vulgaris strains of various origin haemolyzed 100-50% of erythrocytes. Except for Serratia, the other representatives of Enterobacteriaceae did not demonstrate such activity in the same conditions. The preliminary characteristics of this phenomenon is given.

Animals↗
PubMed1980

Phenol-extracted lipopeptidopoly-saccharide (LPPS) complex from Listeria monocytogenes.

Endotoxin phenol extraction method with subsequent ultracentrifugation and/or chromatographic analysis on Sepharose 2 B column were used to obtain biologically active isolate that turned out to contain polysaccharide, peptide and lipid fractions. The raw phenol extract formed 15% and the LPPS complex, obtained from it by ultracentrifugation, 0.17% of bacterial biomass. The LPPS complex contained 11 amino acids representing about 11% of its dry weight. Similarly as in factor Ei and in analogous extracts isolated by other authors the prevailing amino acids were glutamic acid, aspartic acid and lysine. The LPPS complex contained 1.26% of hexosamine, further hexoses, methyl pentoses and ribose. KDO was not detected. Further this complex consisted of 3% of freely-bound and 5% of firmly-bound lipids, beta-hydroxymyrist acid was not detectable. The composition of fatty acids in the firmly-bound lipid fraction of the LPPS complex differed quantitatively from that both in factor Ei and bacterial cell bodies. The tightness of lipid bonds during purification and the biological role of the Listeria lipids are discussed. On the basis of detected chemical and biological properties, both compatible and incompatible with peptidoglycan, a specific character of endotoxin-like isolates from L. monocytogenes is assumed.

Amino Acids↗
PubMed1977

Ribitol-containing lipopolysaccharides from Proteus mirabilis and their serological relationship.

Ribitol phosphate was recently identified as a constituent of lipopolysaccharides obtained from 'proteus mirabilis strain D52 giving 1:4-anhydroribitol during acid hydrolysis (Gmeiner, 1975). Two other Proteus mirabilis strains belonging to serogroups O16 and O33 were shown previously to contain an unknown compoound X as lipopolysaccharide constituent (Kotelko et al., 1975). In this report the identification of compound X as 1:4-anhydroribotol by gas-liquid chromatography, mass spectrometry and mass fragmentography is described. Serological investigations using passive hemagglutination, hemagglutination inhbition and semi-quantitative precipitin reactions indicate strongly that ribitol plays a role in the serological specificity of the respective lipopolysaccharides.

Hemagglutination Inhibition Tests↗