Detection of Fibrinolytic and Elastase Activity Among Clinical Isolates of &lt;i&gt;Serratia Marcescen&lt;/i&gt;&lt;i&gt;s&lt;/i&gt;

Traub, Walter H.; Kleber, Ingrid

doi:10.1159/000162708

Cited by 5 publications

(3 citation statements)

References 16 publications

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“…As exemplified by the diverging fibrinolytic abilities of the 5 strains of S. faecalis, interstrain intraspecies variation occurred and was associated with diverging results of the gelatin liquefaction test. For S. marcescens, others have found a similar correlation between gelatin liquefac tion and fibrinolytic enzymatic activity [12], These authors suggested that the gelatinase and 'fibrinolysin' of S. marcescens possibly are the same enzyme.…”

Section: Discussionmentioning

confidence: 84%

Bacterial Lysis of Fibrin Seal in vitro

Hoffmann

Moesgaard²

1988

Eur Surg Res

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We performed an in vitro study to determine whether certain bacteria may lyse a commercially available fibrin seal (Beriplast®, Behringwerke, Marburg, FRG). Fibrinogen solution was mixed with actively growing bacterial cultures, and thrombin was added. During 20 days of incubation at 37 °C complete lysis was observed with a number of different bacteria, however, at different rates. Complete lysis within 1–5 days was observed for the following species (number of strains in parentheses): Streptococcus faecalis (3), Pseudomonas aeruginosa (2), Serratia marcescens (2), and Serratia liquefaciens (1). Lysis was observed after 6–10 days for Enterobacter cloacae (2), Morganella morganii (2), Escherichia coli (2), S. marcescens (1), and Klebsiella pneumoniae (2). Lysis after 11–16 days was observed for Streptococcus pyogenes (2), S. faecalis (2), and Staphylococcus aureus (2). Rapid lysis was associated with the ability of the strain to liquefy gelatin, i.e. the production of a protease.

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Section: Discussionmentioning

confidence: 84%

Bacterial Lysis of Fibrin Seal in vitro

Hoffmann

Moesgaard²

1988

Eur Surg Res

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“…Examinations of other S. marcescens strains, by four other groups of investigators, support the idea that many strains ofS. marcescens can elaborate several extracellular proteases which differ from one another with regard to their substrate specificities (49), pH optima (22), sensitivities to inactivation by EDTA and DFP (22), isoelectric points (50), and electrophoretic mobilities in agarose gel (19). Additional studies are needed to isolate, characterize, and compare the different proteases of S. marcescens.…”

Section: Resultsmentioning

confidence: 97%

Purification and Characterization of a Serratia marcescens Metalloprotease

Lyerly

Kreger

1979

Infect Immun

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An extracellular, nonelastolytic, neutral metalloprotease of Serratia marcescens was purified by sequential ammonium sulfate precipitation, hydroxyapatite adsorption chromatography, flat-bed isoelectric focusing, and Sephadex G-100 gel filtration. The protease preparation had a 280/260 nm absorbance ratio of 1.8, was free of detectable amounts of endotoxin, carbohydrate, phosphorus, and other known extracellular enzymes of S. marcescens, and was homogeneous by Ouchterlony double immunodiffusion and Grabar-Williams immunoelectrophoresis. Crossed immunoelectrophoresis, thin-layer electrofocusing in polyacrylamide gel, and polyacrylamide disc gel electrophoresis showed three to four closely migrating, Coomassie blue-staining components in the protease preparation. However, zymogram analyses of the patterns showed that protease activity was associated with each component and that the protease was, therefore, microheterogeneous. The isoelectric point and sedimentation coefficient of the protease were approximately 5.3 to 5.4 and 4.2S, respectively, and the molecular weight estimated by sodium dodecyl sulfate-polyacrylanide gel electrophoresis and by gel filtration was approximately 52,500 and 44,000, respectively. The pH optimum range, with azocasein as the substrate, was 5.5 to 7.5. The enzyme contained a high percentage genesis of S. marcescens keratitis and pneumonia, therefore, prompted us to develop a purifi-411 on August 1, 2020 by guest

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“…Until recently, the haemolytic activity of Serratia marcescens strains was the subject of interest in only few papers [3][4][5]11,12]. Profound studies of this activity were performed by Braun et al [1,2,6,7] who found the lytic substance cell-bound.…”

Section: Introductionmentioning

confidence: 99%

Extracellular haemolytic activity of Serratia marcescens

Goluszko¹

1989

FEMS Microbiology Letters

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Blood agar medium with dialysis membrane mounted between two layers of agar was applied to study the haemolytic activity of 28 strains of Serratia marcescens. Two kinds of lytic substances differing with their ability to pass through dialysis membrane were found. Haemolytic activity was not detected in cell-free filtrates from liquid cultures. The discrepancies between haemolytic activity in blood agar media and activity of liquid cultures were observed. Stable attachment of bacterial cells to the erythrocytes was not necessary to lysis. The possibility of extracellular haemolysin is discussed.

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Detection of Fibrinolytic and Elastase Activity Among Clinical Isolates of <i>Serratia Marcescen</i><i>s</i>

Cited by 5 publications

References 16 publications

Bacterial Lysis of Fibrin Seal in vitro

Bacterial Lysis of Fibrin Seal in vitro

Purification and Characterization of a Serratia marcescens Metalloprotease

Extracellular haemolytic activity of Serratia marcescens

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