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MLST was performed on all the strains by sequencing the internal fragments of seven housekeeping genes (arcC, aroE, glpF, gmK, pta, tpi, and yqiL).
This was tested by subjecting a glpF allele 321 sample to PCR in LCGreenPlus master mix, making a dilution series of the reaction products in the same master mix, and then subjecting the dilutions to HRMA.
Randomly selecting some points of both blank and GLPF, their thicknesses were tested by step profiler and the average thickness was calculated as well.
The GenBank accession numbers of staphylococcal gene sequences, arcC, aroe, glpf, gmk, pta, tpi, and yqil, determined in this study were, respectively, JF495119, JF495120, JF495121, JF495122, JF495123, JF495124, and JF495125.
We performed MLST analysis on Elc2, first by analyzing the genomic data, and subsequently, by Sanger-sequencing internal fragments of 7 housekeeping genes (glpF, gmk, ilvD, pta, pur, pycA, and tpi).
We previously identified the Escherichia coli aquaglyceroporin GlpF as a channel for As(III) and trivalent inorganic antimony [Sb(III)] (Meng et al.
Based upon these initial results, World Water Works communicated to GLPF that it might be possible to only run one M80FP pump for each 125 hp Poseipump, but with a 40 HP motor and achieve the desired treatment results.
This work was part of a larger project funded by the GLPF, and coordinated by Larry Brown of the OSU.
A model of the coelacanth Aqp3 channel based upon the structure mask of the bacterial glycerol uptake facilitator (GlpF) (Protein Data Bank 1LDF) illustrates that this more relaxed structure is also a conserved feature of Glps (Fig.
To further investigate the genetic basis of the strain, multilocus sequence typing (MLST), a method that uses seven housekeeping genes (arcC, aroE, glpF, gmk, pta, tpi and yqiL) for genetic identification, and result was assigned by comparison with the S.
The sequences for the loci glpF, gmk, ilvD, pta, pur, pycA, and tpi were then assigned allele designations.
The PfAQP protein sequence is highly similar to that of the Escherichia coli glycerol facilitator GlpF (having 50% similar and 35% identical residues; Hansen et al., 2002), suggesting that in the malaria parasite a bifunctional solute channel of bacterial origin has evolved (Beitz, 2005).
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