scholarly journals Typing of ΦSP–3 lytic Salmonella bacteriophages obtained from various fecal sources

2020 ◽  
Vol 44 (5) ◽  
pp. 1047-1054
Author(s):  
Aslı SAKMANOĞLU ◽  
Hasan Hüseyin HADİMLİ
Keyword(s):  
Host Range ◽  
Dairy Cow ◽  
Lytic Activity ◽  
Multiplicity Of Infection ◽  
Fecal Samples ◽  
Activity Assessment ◽  
Sds Page ◽  
The Cross ◽  
Discriminatory Index

Although several reports are available on both ΦSP–1 and ΦSP–3 lytic Salmonella bacteriophages obtained from poultry, further research is required to study the effectiveness of ΦSP–3 type on serovars isolated from other sources. In the present study, we aimed to isolate bacteriophages from 8 serovars previously obtained from 869 fecal samples (calf, dairy cow, buffalo, and camel), genotype the bacteriophages, and detect the cross-lytic activities of the bacteriophages on Salmonella enterica subsp. enterica serovar Kentucky, S.Anatum, and S.Muenchen. A total of 16 bacteriophages were detected as ΦSP–3 type via PCR. The Hunter-Gaston Discriminatory Index of SDS-PAGE was calculated to be 0.825. Determination of multiplicity of infection (MOI) values were different for each bacteriophage according to the cross-lytic activity assessment. The MOI of the most effective S. Kentucky bacteriophage was 79.11 μg/mL for 2.5×104 cells, whereas that of the most ineffective S.Muenchen bacteriophage was 1.142 μg/μL for 2.5×104 cells. In conclusion, it was assumed that owing to the high and cross-lytic activity of the S. Kentucky bacteriophage, it has a larger host range, which differs in the lytic activities of each bacteriophage, despite being the same serovar, and that calf feces is the most important source for obtaining Salmonella bacteriophages.

Characterization of Glycoprotein Fraction from Carp Pituitaries Isolated Using Concanavalin A as the Affinity Ligand

1998 ◽  
Vol 63 (3) ◽  
pp. 434-440 ◽  
Author(s):  
Irena Hulová ◽  
Jana Barthová ◽  
Helena Ryšlavá ◽  
Václav Kašička
Keyword(s):  
Concanavalin A ◽  
Reversed Phase ◽  
Amino Acid Sequences ◽  
Gel Chromatography ◽  
Affinity Ligand ◽  
Sds Page ◽  
Terminal Amino ◽  
Α And Β Subunits

Glycoproteins that have affinity to Concanavalin A were isolated from the acetone-dried pituitaries of common carp (Cyprinus carpio L.). Two fractions of glycoproteins were separated using gel chromatography on Superdex 75HR. The fraction with lower molecular weight (30 000) corresponding to the carp gonadotropin cGtH II was composed of two subunits as determined using SDS-PAGE. This protein fraction was further divided into four components using reversed-phase HPLC. Two fractions were pure α and β subunits of cGtH II as follows from immunodetection and from determination of N-terminal amino acid sequences. The other two were a mixture of α and β subunits as was also revealed by N-terminal analysis. Capillary electrophoresis was also used for characterization of isolated glycoproteins.

scholarly journals Alignment determination of the Hayabusa2 laser altimeter (LIDAR)

2021 ◽  
Vol 73 (1) ◽  
Author(s):  
Hirotomo Noda ◽  
Hiroki Senshu ◽  
Koji Matsumoto ◽  
Noriyuki Namiki ◽  
Takahide Mizuno ◽  
...  
Keyword(s):  
Altimeter Data ◽  
Gravity Assist ◽  
Laser Altimeter ◽  
Trajectory Error ◽  
Flight Data ◽  
Camera Image ◽  
Operation Period ◽  
The Cross ◽  
Along Track

AbstractIn this study, we determined the alignment of the laser altimeter aboard Hayabusa2 with respect to the spacecraft using in-flight data. Since the laser altimeter data were used to estimate the trajectory of the Hayabusa2 spacecraft, the pointing direction of the altimeter needed to be accurately determined. The boresight direction of the receiving telescope was estimated by comparing elevations of the laser altimeter data and camera images, and was confirmed by identifying prominent terrains of other datasets. The estimated boresight direction obtained by the laser link experiment in the winter of 2015, during the Earth’s gravity assist operation period, differed from the direction estimated in this study, which fell on another part of the candidate direction; this was not selected in a previous study. Assuming that the uncertainty of alignment determination of the laser altimeter boresight was 4.6 pixels in the camera image, the trajectory error of the spacecraft in the cross- and/or along-track directions was determined to be 0.4, 2.1, or 8.6 m for altitudes of 1, 5, or 20 km, respectively.

scholarly journals Isolation and characterization of pathogenic Escherichia coli bacteriophages from chicken and beef offal

2020 ◽  
Vol 13 (1) ◽  
Author(s):  
Celosia Lukman ◽  
Christopher Yonathan ◽  
Stella Magdalena ◽  
Diana Elizabeth Waturangi
Keyword(s):  
Escherichia Coli ◽  
Foodborne Pathogens ◽  
High Efficiency ◽  
Multiplicity Of Infection ◽  
Isolation And Characterization ◽  
Transmission Electron ◽  
Pathogenic Escherichia Coli ◽  
Family Based

Abstract Objective This study was conducted to isolate and characterize lytic bacteriophages for pathogenic Escherichia coli from chicken and beef offal, and analyze their capability as biocontrol for several foodborne pathogens. Methods done in this research are bacteriophage isolation, purification, titer determination, application, determination of host range and minimum multiplicity of infection (miMOI), and bacteriophage morphology. Results Six bacteriophages successfully isolated from chicken and beef offal using EPEC and EHEC as host strain. Bacteriophage titers observed between 109 and 1010 PFU mL−1. CS EPEC and BL EHEC bacteriophage showed high efficiency in reduction of EPEC or EHEC contamination in meat about 99.20% and 99.04%. The lowest miMOI was 0.01 showed by CS EPEC bacteriophage. CI EPEC and BL EPEC bacteriophage suspected as Myoviridae family based on its micrograph from Transmission Electron Microscopy (TEM). Refers to their activity, bacteriophages isolated in this study have a great potential to be used as biocontrol against several foodborne pathogens.

Studies on the Organisation of Glycoproteins and Proteins in Human Platelet Membranes

1979 ◽  
Author(s):  
A.T. Nurden ◽  
D. Dupuis ◽  
H. de la Baume ◽  
J.P. Caen
Keyword(s):  
Human Platelet ◽  
Membrane Vesicles ◽  
Human Platelets ◽  
Cross Linking ◽  
Platelet Response ◽  
Membrane Glycoproteins ◽  
Sh Groups ◽  
Sds Page ◽  
The Cross ◽  
Neighbour Analysis

Addition of wheat germ agglutinin (WGA) (50 ug/ml) to washed human platelets (3 x 108/ml) resulted in platelet activation and the release of l4C-5HT within the same time scale as 0.05 units/ml thrombin. In contrast, succinyl-WGA (100 ug/ml) induced no platelet response. The increased valency of WGA (4) compared with succinyl-WGA (2) suggests that the activation is induced through the cross-linking (immobilisation ?) of closely associated receptors in the membrane. This finding induced us to attempt to cross-link and thereby identify adjacent molecules in the membrane by “near-neighbour” analysis. Constituent -SH groups were oxidised employing Cu2+/phenanthroline or diamide as catalysts, and polymers formed as a result of intermolecular -S-S- formation between adjacent molecules were identified by SDS-PAGE. Although previous reports have shown that the major human platelet membrane glycoproteins contain -SH groups, no apparent cross-linking of the glycoproteins was located following the incubation of either washed platelets or isolated membranes with Cu2+/phenanthroline or diamide. However bidimensional SDS-PAGE (1st dimension non-reduced, 2nd dimension reduced) showed the presence of several protein polymers including complexes formed by the cross-linking of 3 large polypeptides of M. Wt. 250 000, 220 000 and 200 000. These components were easily eluted from membrane vesicles at pH 10 and may represent closely associated constituents at the cytoplasmic surface of the plasma membrane.

Determination of the cross section forTb159(n,2n)Tb158and the half-life ofTb158

1984 ◽  
Vol 30 (3) ◽  
pp. 823-825 ◽  
Author(s):  
R. J. Prestwood ◽  
D. B. Curtis ◽  
D. J. Rokop ◽  
D. R. Nethaway ◽  
N. L. Smith
Keyword(s):  
Cross Section ◽  
Half Life ◽  
The Cross

scholarly journals Escherichia coli is not a suitable fecal indicator to assess water fecal contamination by otters

2017 ◽  
Vol 78 (1) ◽  
pp. 155-159 ◽  
Author(s):  
M. Oliveira ◽  
D. Freire ◽  
N. M. Pedroso
Keyword(s):  
Escherichia Coli ◽  
Fecal Contamination ◽  
Microbiological Quality ◽  
Aquatic Environments ◽  
Pathogenic Microorganisms ◽  
Fecal Indicator ◽  
Fecal Samples ◽  
E Coli ◽  
Paulo State

Abstract The detection of pathogenic microorganisms in aquatic environments is extremely relevant in terms of public health. As these laboratorial methodologies are usually difficult, expensive and time-consuming, they are frequently replaced by the assessment of fecal indicator bacteria, such as Escherichia coli. This study aimed to assess the presence of E. coli in fecal samples from Neotropical otters, to evaluate its potential as fecal indicator to be applied to the determination of water microbiological quality in areas where otters’ populations are high. Twenty-six otter fecal samples, collected in Alto Paranapanema river basin, São Paulo State, Brazil, were analyzed for the presence of E. coli, using conventional bacteriological methods. Only 8 scat samples (30%) were E. coli positive, indicating that this microorganism is not a suitable fecal indicator to assess water fecal contamination by Neotropical otters, and should not be used to infer the presence of otter related pathogens in waters.

Cross-Reactivity between IgE-Binding Proteins from Anisakis Simplex and Dermatophagoides Pteronyssinus

2005 ◽  
Vol 18 (4) ◽  
pp. 671-675 ◽  
Author(s):  
R. Bernardini ◽  
G. Mistrello ◽  
E. Novembre ◽  
D. Roncarolo ◽  
S. Zanotta ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Binding Proteins ◽  
Specific Ige ◽  
Dermatophagoides Pteronyssinus ◽  
Cross Reactivity ◽  
Anisakis Simplex ◽  
Cross Reaction ◽  
Ige Binding ◽  
Sds Page ◽  
The Cross

An association was found between Anisakis simplex (As) and Dermatophagoides pteronyssinus (Dp) sensitization. One recent study shows a cross-reactivity between As and Dp and tropomyosin (tr) is suspected as being one of the proteins responsible of this cross-reaction. The aim of our study was: 1) to confirm the cross-reactivity between Dp and As; 2) to determine the importance of tr in this cross reaction. SDS-PAGE analysis of Dp and As (metabolic and somatic) extracts was carried out. Then an IgE immunoblotting test using serum from a patient who had specific IgE only to Dp and As and immunoblotting inhibition experiments using Dp extract and tr as inhibitors were performed. We found that patient's serum reacted: 1) against larval As antigens with a molecular weight (mw) of 25 kilodalton (kD) and a mw > 100 kD, 2) against various metabolic As antigens with a mw > 100 kD, a mw ranging approximately from 35 to 50 kD, and a mw around 20 kD, and 3) against Dp proteins with mw between 35 and 55 kD. Preincubation of patient's serum with Dp extract caused the disappearance of reactivity against antigens with a mw > 100 kD in both larval and metabolic As extracts and against proteins with mw ranging approximately from 35 to 50 kD in the metabolic As extract. Preincubation of patient's serum with As extract caused the disappearance of reactivity against antigens with mw between 35 and 55 kD in the Dp extract. Pre-incubation of patient's serum with tr did not induce any change in the immunoblotting profile. The results show that 1) cross-reactive components between Dp and As are some proteins with a mw ranging approximately from 35 to 50 kD and with a mw > 100 kD, and 2) tr is not involved in cross-reactivity between As and Dp.

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