scholarly journals Comparison of lipopolysaccharides from Agmenellum quadruplicatum to Escherichia coli and Salmonella typhimurium by using thin-layer chromatography.

1975 ◽  
Vol 124 (3) ◽  
pp. 1566-1573 ◽  
Author(s):  
T M Buttke ◽  
L O Ingram
Keyword(s):  
Escherichia Coli ◽  
Thin Layer ◽  
Salmonella Typhimurium ◽  
Thin Layer Chromatography ◽  
Agmenellum Quadruplicatum ◽  
Layer Chromatography

scholarly journals ANTIBACTERIAL ACTIVITY AND THIN LAYER CHROMATOGRAPHY PROFILE Muntingia Calabura LEAF EXTRACT AS A MATERIAL CANDIDATE HAND SANITIZER

2018 ◽  
Vol 11 (1) ◽  
pp. 43
Author(s):  
Santy Pristianingrum ◽  
Baiq Lely Zainiati ◽  
Iwan Doddy Dharmawibawa
Keyword(s):  
Escherichia Coli ◽  
Staphylococcus Aureus ◽  
Pseudomonas Aeruginosa ◽  
Thin Layer ◽  
Thin Layer Chromatography ◽  
Preventive Action ◽  
Hand Sanitizer ◽  
Layer Chromatography ◽  
Active Substances ◽  
Muntingia Calabura

Abstract : the utilization of antibacterial active substances from several plants is increasingly not only as the ingredients of medicine, but its utilization is also utilized for an antibacterial ingredient for preventive action, one of them is hand sanitizer material. This research focused to find the antibacterial active substances alternative from Muntingia calabura leaves extract. The data were analyzed descriptively including the inhibitory of ethanol absolute extract and ethanol 95% of M. Calabura against isolate clinical bacteria by Kirby Bauer method and the type of coumpund that contains in M.calabura leaf by thin layer chromatography utilizingeluen n-hexan- Methanol. Etanol absolute extract M.calabura leaf showing the average inhibition zone against Pseudomonas aeruginosa 15.67 mm, Staphylococcus aureus 19.33 mm and Escherichia coli 13 mm. While, The etanol extract 95% showing higher inhibition Pseudomonas aeruginosa 19.67 mm, Staphylococcus aureus 19.33 mm and Escherichia coli 16.67 mm. This inhibitory zone was slightly lower than chlorhexidine gluconate with an average of 20-24 mm against the three bacteria that utilized in the test but belongs to the strongly sensitive category for natural materials according to Mukherjee (1988). From thin layer chromatography profile with eluen n-hexan: methanol found three compounds that were in the range of Rf value 0.4; 0.5 and 0.7. The Conclusion for this study is the bioactive material from etanol 95% extract M.calabura leaf can be optimized to the hand sanitizer active compound candidate.

scholarly journals Identification of a Novel 6′-N-Aminoglycoside Acetyltransferase, AAC(6′)-Iak, from a Multidrug-Resistant Clinical Isolate of Stenotrophomonas maltophilia

2014 ◽  
Vol 58 (10) ◽  
pp. 6324-6327 ◽  
Author(s):  
Tatsuya Tada ◽  
Tohru Miyoshi-Akiyama ◽  
Rajan K. Dahal ◽  
Shyam K. Mishra ◽  
Kayo Shimada ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Thin Layer ◽  
Thin Layer Chromatography ◽  
Clinical Isolate ◽  
Stenotrophomonas Maltophilia ◽  
Multidrug Resistant ◽  
Content Type ◽  
Encoding Gene ◽  
Layer Chromatography

ABSTRACTStenotrophomonas maltophiliaIOMTU250 has a novel 6′-N-aminoglycoside acetyltransferase-encoding gene,aac(6′)-Iak. The encoded protein, AAC(6′)-Iak, consists of 153 amino acids and has 86.3% identity to AAC(6′)-Iz.Escherichia colitransformed with a plasmid containingaac(6′)-Iakexhibited decreased susceptibility to arbekacin, dibekacin, neomycin, netilmicin, sisomicin, and tobramycin. Thin-layer chromatography showed that AAC(6′)-Iak acetylated amikacin, arbekacin, dibekacin, isepamicin, kanamycin, neomycin, netilmicin, sisomicin, and tobramycin but not apramycin, gentamicin, or lividomycin.

scholarly journals Antibacterial Activity of Lidah Mertua (Sansevieria Trifasciata Prain.) Leaves Extract on Escherichia coli and Staphylococcus aureus

2019 ◽  
Vol 7 (22) ◽  
pp. 3882-3886
Author(s):  
Yessi Febriani ◽  
Vriezka Mierza ◽  
Novi Putri Handayani ◽  
Surismayanti Surismayanti ◽  
Ibrenaita Ginting
Keyword(s):  
Escherichia Coli ◽  
Antibacterial Activity ◽  
Thin Layer ◽  
Thin Layer Chromatography ◽  
Chemical Compounds ◽  
Inhibition Zone ◽  
Chromatography Method ◽  
E Coli ◽  
Layer Chromatography ◽  
And Staphylococcus Aureus

BACKGROUND: Infection is the most common diseases in developing country, including Indonesia. Bacteria that often causes infection is Escherichia coli and Staphylococcus aureus. One of the traditional plants that can be used as an antibacterial is lidah mertua. AIM: The purpose of this study was to find out the profile of chemical compounds by thin layer chromatography method and determine the antibacterial activity of Lidah Mertua leaves by in vitro. METHODS: This research conducted an experimentally using non-polar, semipolar, and polar as solvents to get extract against E. coli and S. aureus as bacterial testing. The antibacterial activity using agar diffusion method to get minimum inhibitory concentration (MIC). RESULTS: The result of the research on thin layer chromatography showed that the compounds contained in the Lidah Mertua leaves were polifenol, steroids and alkaloids. The data obtained were tabulated and analysed descriptively. The antibacterial activity show that n-hexane extract does not provide inhibitory activity. MIC value show that aethyl acetate extract of lidah mertua leaves inhibited the growth of E. coli and S. aureus at concentration 50 mg/mL and 25 mg/mL with diameters of inhibition zone is 8.50 mm and 8.20 mm and methanol extract of lidah mertua leaves inhibited the growth of E. coli and S. aureus at concentration 12.5 mg/mL and 25 mg/mL with diameters of inhibition zone is 8.46 mm and 8.32 mm. CONCLUSION: The profile of chemical compounds by thin layer chromatography method showed that the compounds contained in the Lidah Mertua leaves were polifenol, steroids and alkaloids. The antibacterial activity show that n-hexane extract does not provide inhibitory activity, but aethyl acetate extract of lidah mertua leaves inhibited the growth of E. coli and S. aureus.

scholarly journals The pH 6 Antigen of Yersinia pestisBinds to β1-Linked Galactosyl Residues in Glycosphingolipids

1998 ◽  
Vol 66 (9) ◽  
pp. 4545-4548 ◽  
Author(s):  
Dean Payne ◽  
David Tatham ◽  
E. Diane Williamson ◽  
Richard W. Titball
Keyword(s):  
Escherichia Coli ◽  
Thin Layer ◽  
Yersinia Pestis ◽  
Thin Layer Chromatography ◽  
E Coli ◽  
Maximal Binding ◽  
Layer Chromatography ◽  
Overlay Assay ◽  
Galactosyl Residues

ABSTRACT The Yersinia pestis pH 6 antigen was expressed by, and purified from, Escherichia coli containing cloned psa genes. By an enzyme-linked immunosorbence-based assay, purified pH 6 antigen bound to gangliotetraosylceramide (GM1A), gangliotriaosylceramide (GM2A), and lactosylceramide (LC) (designations follow the nomenclature of L. Svennerholm [J. Neurochem. 10:613–623, 1963]). Binding to GM1A, GM2A, and LC was saturable, with 50% maximal binding occurring at 498 ± 4, 390, and 196 ± 3 nM, respectively. Thin-layer chromatography (TLC) overlay binding confirmed that purified pH 6 antigen bound to GM1A, GM2A, and LC and also revealed binding to hydroxylated galactosylceramide. Intact E. coli cells which expressed the pH 6 antigen had a specificity similar to that of purified pH 6 in the TLC overlay assay except that nonhydroxylated galactosylceramide was also bound. The binding patterns observed indicate that the presence of β1-linked galactosyl residues in glycosphingolipids is the minimum determinant required for binding of the pH 6 antigen.

scholarly journals Vibrio harveyi Nitroreductase Is Also a Chromate Reductase

2003 ◽  
Vol 69 (8) ◽  
pp. 4390-4395 ◽  
Author(s):  
Young Hak Kwak ◽  
Dong Seok Lee ◽  
Han Bok Kim
Keyword(s):  
Escherichia Coli ◽  
Thin Layer ◽  
Molecular Mass ◽  
Thin Layer Chromatography ◽  
Vibrio Harveyi ◽  
Chromate Reduction ◽  
E Coli ◽  
Chromate Reductase ◽  
Layer Chromatography ◽  
Chromate Reductases

ABSTRACT The chromate reductase purified from Pseudomonas ambigua was found to be homologous with several nitroreductases. Escherichia coli DH5α and Vibrio harveyi KCTC 2720 nitroreductases were chosen for the present study, and their chromate-reducing activities were determined. A fusion between glutathione S-transferase (GST) and E. coli DH5α NfsA (GST-EcNfsA), a fusion between GST and E. coli DH5α NfsB (GST-EcNfsB), and a fusion between GST and V. harveyi KCTC 2720 NfsA (GST-VhNfsA) were prepared for their overproduction and easy purification. GST-EcNfsA, GST-EcNFsB, and GST-VhNFsA efficiently reduced nitrofurazone and 2,4,6-trinitrotoluene (TNT) as their nitro substrates. The Km values for GST-EcNfsA, GST-EcNfsB, and GST-VhNfsA for chromate reduction were 11.8, 23.5, and 5.4 μM, respectively. The V max values for GST-EcNfsA, GST-EcNfsB, and GST-VhNfsA were 3.8, 3.9, and 10.7 nmol/min/mg of protein, respectively. GST-VhNfsA was the most effective of the three chromate reductases, as determined by each V max/Km value. The optimal temperatures of GST-EcNfsA, GST-EcNfsB, and GST-VhNfsA for chromate reduction were 55, 30, and 30°C, respectively. Thus, it is confirmed that nitroreductase can also act as a chromate reductase. Nitroreductases may be used in chromate remediation. GST-EcNfsA, GST-EcNfsB, and GST-VhNfsA have a molecular mass of 50 kDa and exist as a monomer in solution. Thin-layer chromatography showed that GST-EcNfsA, GST-EcNfsB, and GST-VhNfsA contain FMN as a cofactor. GST-VhNfsA reduced Cr(VI) to Cr(III). Cr(III) was much less toxic to E. coli than Cr(VI).

scholarly journals Effect of Slow Growth on Metabolism of Escherichia coli, as Revealed by Global Metabolite Pool (“Metabolome”) Analysis

1998 ◽  
Vol 180 (19) ◽  
pp. 5109-5116 ◽  
Author(s):  
Helen Tweeddale ◽  
Lucinda Notley-McRobb ◽  
Thomas Ferenci
Keyword(s):  
Escherichia Coli ◽  
Thin Layer ◽  
Thin Layer Chromatography ◽  
Growth Rates ◽  
Slow Growth ◽  
Two Dimensional ◽  
Metabolome Analysis ◽  
Metabolic Genes ◽  
Metabolite Pool ◽  
Layer Chromatography

ABSTRACT Escherichia coli growing on glucose in minimal medium controls its metabolite pools in response to environmental conditions. The extent of pool changes was followed through two-dimensional thin-layer chromatography of all 14C-glucose labelled compounds extracted from bacteria. The patterns of metabolites and spot intensities detected by phosphorimaging were found to reproducibly differ depending on culture conditions. Clear trends were apparent in the pool sizes of several of the 70 most abundant metabolites extracted from bacteria growing in glucose-limited chemostats at different growth rates. The pools of glutamate, aspartate, trehalose, and adenosine as well as UDP-sugars and putrescine changed markedly. The data on pools observed by two-dimensional thin-layer chromatography were confirmed for amino acids by independent analysis. Other unidentified metabolites also displayed different spot intensities under various conditions, with four trend patterns depending on growth rate. As RpoS controls a number of metabolic genes in response to nutrient limitation, anrpoS mutant was also analyzed for metabolite pools. The mutant had altered metabolite profiles, but only some of the changes at slow growth rates were ascribable to the known control of metabolic genes by RpoS. These results indicate that total metabolite pool (“metabolome”) analysis offers a means of revealing novel aspects of cellular metabolism and global regulation.

scholarly journals The mdoC Gene of Escherichia coli Encodes a Membrane Protein That Is Required for Succinylation of Osmoregulated Periplasmic Glucans

1999 ◽  
Vol 181 (12) ◽  
pp. 3626-3631 ◽  
Author(s):  
Jean-Marie Lacroix ◽  
Eric Lanfroy ◽  
Virginie Cogez ◽  
Yannick Lequette ◽  
Anne Bohin ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Membrane Protein ◽  
Thin Layer ◽  
Thin Layer Chromatography ◽  
Unknown Origin ◽  
Periplasmic Space ◽  
Membrane Phospholipids ◽  
Membrane Bound ◽  
Layer Chromatography ◽  
Putative Mutant

ABSTRACT Osmoregulated periplasmic glucans (OPGs) of Escherichia coli are anionic oligosaccharides that accumulate in the periplasmic space in response to low osmolarity of the medium. Their anionic character is provided by the substitution of the glucosidic backbone by phosphoglycerol originating from the membrane phospholipids and by succinyl residues from unknown origin. A phosphoglycerol-transferase-deficient mdoB mutant was subjected to Tn5 transposon mutagenesis, and putative mutant clones were screened for changes in the anionic character of OPGs by thin-layer chromatography. One mutant deficient in succinylation of OPGs was obtained, and the gene inactivated in this mutant was characterized and named mdoC. mdoC, which encodes a membrane-bound protein, is closely linked to themdoGH operon necessary for the synthesis of the OPG backbone.

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