Journal:

Article Title: ampR Gene Mutations That Greatly Increase Class C ?-Lactamase Activity in Enterobacter cloacae

doi:

Figure Lengend Snippet: β-Lactamase activity

Article Snippet: Table shows that the β-lactamase activities of the pKU411 transformants were almost the same as those of the host strains, whereas the activities of the pKU412, pKU413, and pKU415 transformants were 20 to 350 times, 10 to 130 times, and 15 to 250 times higher, respectively. table ft1 table-wrap mode="anchored" t5 TABLE 4 caption a7 Plasmid β-Lactamase activity (U/mg of protein) a KU3261 KU3262 KU3263 ATCC 13047 <0.02 0.06 <0.02 0.07 pKU411 0.02 0.03 <0.02 0.06 pKU412 6.96 6.40 1.72 1.38 pKU413 2.56 2.01 0.34 0.78 pKU415 4.82 4.34 0.93 1.07 Open in a separate window a One unit of β-lactamase activity was defined as the amount of β-lactamase that hydrolyzed 1 μmol of cephalothin in 1 min at 30°C.

Techniques: Plasmid Preparation, Activity Assay, Mutagenesis

Journal:

Article Title: ampR Gene Mutations That Greatly Increase Class C ?-Lactamase Activity in Enterobacter cloacae

doi:

Figure Lengend Snippet: Effects of AmpR mutants against production of class C β-lactamase in E. cloacae ATCC 13047 and three clinical isolates

Article Snippet: Table shows that the β-lactamase activities of the pKU411 transformants were almost the same as those of the host strains, whereas the activities of the pKU412, pKU413, and pKU415 transformants were 20 to 350 times, 10 to 130 times, and 15 to 250 times higher, respectively. table ft1 table-wrap mode="anchored" t5 TABLE 4 caption a7 Plasmid β-Lactamase activity (U/mg of protein) a KU3261 KU3262 KU3263 ATCC 13047 <0.02 0.06 <0.02 0.07 pKU411 0.02 0.03 <0.02 0.06 pKU412 6.96 6.40 1.72 1.38 pKU413 2.56 2.01 0.34 0.78 pKU415 4.82 4.34 0.93 1.07 Open in a separate window a One unit of β-lactamase activity was defined as the amount of β-lactamase that hydrolyzed 1 μmol of cephalothin in 1 min at 30°C.

Techniques: Activity Assay

Journal: Molecular therapy : the journal of the American Society of Gene Therapy

Article Title: Preferential transduction of human hepatocytes with lentiviral vectors pseudotyped by Sendai virus F protein.

doi: 10.1006/mthe.2002.0603

Figure Lengend Snippet: FIG. 2. Cell transduction with SV-F pseudotyped HIV vectors. (A–C) HepG2 cells transduced with SV-F pseudotyped HIV- 3/-gal, HIV-6/-gal, and HIV-7/-gal, respectively. The p24 level of each vector preparation was determined and 100 ng p24 was applied for HepG2 transduction. The cells were stained for -gal activity 72 hours after transduction. (D, E) HUVEC transduced with HIV-7/-gal pseudotyped with either VSV-G or SV-F. (F, G) Primary human heptocytes were trans- duced with either HIV-7/-gal(G) or HIV-7/-gal(F). Similar amounts of the vectors, as determined by the p24 level in each vector preparation, were used for transduction. Approximately 160 ng of p24 were used for the transductions.

Article Snippet: 765 TABLE 6: Transduction efficiency of different HIV vectors in HT1080 and HepG2 cells HT1080 HepG2 Vector Titer (TU/ml) -gal activity Titer (TU/ml) -gal activity (U/mg protein extract/ng p24) (U/mg protein extract/ng p24) HIV-3/ -gal 1.4 106 ± 0.1 106 64.3 ± 5.1 2.3 104 ± 0.3 104 5.3 ± 1.2 HIV-6/ -gal 1.7 106 ± 0.1 106 140.4 ± 14.4 3.6 104 ± 0.3 104 28.3 ± 7.1 HIV-7/ -gal 1.9 106 ± 0.2 106 259.1 ± 15.4 1.0 105 ± 0.5 105 123.1 ± 10.1 HIV vectors pseudotyed with VSV-G and SV-F were generated by transient transfection and used for transduction of HT1080 (G) and HepG2 (F) cells.

Techniques: Transduction, Plasmid Preparation, Staining, Activity Assay