scholarly journals Effect of Brominated Furanones on the Formation of Biofilm by Escherichia coli on Polyvinyl Chloride Materials

2013 ◽  
Vol 67 (3) ◽  
pp. 893-897 ◽  
Author(s):  
Ye Lianhua ◽  
Huang Yunchao ◽  
Xu Geng ◽  
Zhou Youquang ◽  
Zhao Guangqiang ◽  
...  
1987 ◽  
Vol 99 (2) ◽  
pp. 323-331 ◽  
Author(s):  
M. G. Smith

SUMMARYSamples of blended mutton tissue in small polyvinyl chloride sachets were incubated in water baths for different times and at varying temperatures. The temperature of each bath was recorded accurately throughout each experiment. Using equations previously derived for the lag and generation times of coliform organisms in blended mutton tissue, the expected increases of these bacteria were calculated from the time/temperature recordings. These were compared with the data obtained from plate counts made on the tissue samples in the sachets before and after incubation. The studies were done with a strain ofEscherichia coli, one ofSalmonella lyphimuriumand the coliform organisms naturally present on sheep carcasses processed in a commercial abattoir. The calculated growth agreed closely with that measured. Therefore, if mutton, after overnight chilling, is warmed again to temperatures within the growth range of these bacteria, the possible increases in the numbers of cells present can be calculated directly from time and temperature measurements.The implications for the present codes of practice in abattoirs are discussed.


MedChemComm ◽  
2013 ◽  
Vol 4 (7) ◽  
pp. 1079 ◽  
Author(s):  
Gauri S. Shetye ◽  
Nischal Singh ◽  
Xiang Gao ◽  
Debjyoti Bandyopadhyay ◽  
Aixin Yan ◽  
...  

Author(s):  
G. Stöffler ◽  
R.W. Bald ◽  
J. Dieckhoff ◽  
H. Eckhard ◽  
R. Lührmann ◽  
...  

A central step towards an understanding of the structure and function of the Escherichia coli ribosome, a large multicomponent assembly, is the elucidation of the spatial arrangement of its 54 proteins and its three rRNA molecules. The structural organization of ribosomal components has been investigated by a number of experimental approaches. Specific antibodies directed against each of the 54 ribosomal proteins of Escherichia coli have been performed to examine antibody-subunit complexes by electron microscopy. The position of the bound antibody, specific for a particular protein, can be determined; it indicates the location of the corresponding protein on the ribosomal surface.The three-dimensional distribution of each of the 21 small subunit proteins on the ribosomal surface has been determined by immuno electron microscopy: the 21 proteins have been found exposed with altogether 43 antibody binding sites. Each one of 12 proteins showed antibody binding at remote positions on the subunit surface, indicating highly extended conformations of the proteins concerned within the 30S ribosomal subunit; the remaining proteins are, however, not necessarily globular in shape (Fig. 1).


Author(s):  
T. G. Gregory

A nondestructive replica technique permitting complete inspection of bore surfaces having an inside diameter from 0.050 inch to 0.500 inch is described. Replicas are thermally formed on the outside surface of plastic tubing inflated in the bore of the sample being studied. This technique provides a new medium for inspection of bores that are too small or otherwise beyond the operating limits of conventional inspection methods.Bore replicas may be prepared by sliding a length of plastic tubing completely through the bore to be studied as shown in Figure 1. Polyvinyl chloride tubing suitable for this replica process is commercially available in sizes from 0.037- to 0.500-inch diameter. A tube size slightly smaller than the bore to be replicated should be used to facilitate insertion of the plastic replica blank into the bore.


Author(s):  
Manfred E. Bayer

Bacterial viruses adsorb specifically to receptors on the host cell surface. Although the chemical composition of some of the cell wall receptors for bacteriophages of the T-series has been described and the number of receptor sites has been estimated to be 150 to 300 per E. coli cell, the localization of the sites on the bacterial wall has been unknown.When logarithmically growing cells of E. coli are transferred into a medium containing 20% sucrose, the cells plasmolize: the protoplast shrinks and becomes separated from the somewhat rigid cell wall. When these cells are fixed in 8% Formaldehyde, post-fixed in OsO4/uranyl acetate, embedded in Vestopal W, then cut in an ultramicrotome and observed with the electron microscope, the separation of protoplast and wall becomes clearly visible, (Fig. 1, 2). At a number of locations however, the protoplasmic membrane adheres to the wall even under the considerable pull of the shrinking protoplast. Thus numerous connecting bridges are maintained between protoplast and cell wall. Estimations of the total number of such wall/membrane associations yield a number of about 300 per cell.


Author(s):  
Manfred E. Bayer

The first step in the infection of a bacterium by a virus consists of a collision between cell and bacteriophage. The presence of virus-specific receptors on the cell surface will trigger a number of events leading eventually to release of the phage nucleic acid. The execution of the various "steps" in the infection process varies from one virus-type to the other, depending on the anatomy of the virus. Small viruses like ØX 174 and MS2 adsorb directly with their capsid to the bacterial receptors, while other phages possess attachment organelles of varying complexity. In bacteriophages T3 (Fig. 1) and T7 the small conical processes of their heads point toward the adsorption site; a welldefined baseplate is attached to the head of P22; heads without baseplates are not infective.


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