As shown in Figure 1a (i), our one-plex SPE-nanoLC-MS chip consists of five key functional modules including a SPE column (blue), a herringbone mixer (brown), a trap column (green), a LC column (red), and an emitter interfaced to a mass spectrometer for nanoelectrospray mass spectrometry.
The clean-up procedure involved a SPE on C18 cartridge.
Shoup addressed the issue by adding a SPE extraction prior to HPLC purification.
Transcarpathian clinoptilolite heated at 350 °C for 2.5 h was applied as a SPE sorbent.
Blood plasma was separated into a polar and non-polar fraction using a SPE method.
Spinning off a subsidiary into a separate publicly traded entity is another way to establish a SPE.
To identify the SAg responsible for the mitogenic activity, PBLs were stimulated with serum 96/2 and serum 99/1, respectively, together with rabbit antibodies against recombinant forms of SPE-A, SPE-C, SPE-G, SPE-J, or SMEZ.
By day 9 after admission (sample 96/2-10), the serum contained high titers of neutralizing antibodies against SPE-A, SPE-C, SPE-I, SSA, SMEZ-1, and SMEZ-2, and a moderate anti SPE-H titer.
On day 3, patient 96/2 had neutralizing antibodies against SPE-A, SPE-C, SPE-I, and SSA but undetectable levels of protective antibodies against SMEZ-1, SMEZ-2, SPE-G, and SPE-H.
Recombinant forms of SPE-A, SPE-C, SPE-G, SPE-H, SPE-I, SPE-J, SSA, SMEZ-1, and SMEZ-2 were produced in Escherichia coli by using the pGEX-2T expression system as described previously (31, 33 ).
Anti SPE-J Anti SPE-JMEZ andiserum were added to PBLs stimulated with vantiserumcombinant SAgs (SPE-A, SPE-C, SPE-G, SPE-H, SPE-I, SPE-J, SMEZ-1, SMEZ-2, and SSA), and results showerethaddedto–SPBLs antibodiestimulatedely inhibited the rSPE-J activity, witheas anti-SMEZ antibodies inhibited the activarious recombinant rSAgs-2.
