Fab fractions

Fa (or Fabs%) Fraction of the oral dose absorbed in vivo/ in humans... 

Sample Fab fraction from HIC separation 15 ml eluate diluted 7.5/100... 

Fab fraction from STREAMLINE SP, 2 ml HiTrap HIC Test Kit (1 ml columns),... 

SpA-Sepharose can also be convenient for the purification of the Fab fragment of IgG. Since this adsorbent retains Fc fragments and complete IgG, the Fab fraction can be recovered free of complete antibody. 

The Fab fraction is eluted in the void volume, concentrated to 5 mg/mL, and treated with a 1/100 volume of DTNB (Ellman reagent) dissolved in DMF (80 mg/mL). 

The luciferin produces a blue oxidation product during its purification process. In the DEAE chromatography of luciferin, this blue compound is eluted before the fractions of luciferin. The fractions of the blue compound were combined and purified by HPLC on a column of Hamilton PRP-1 (7 x 300 mm) using methanol-water (8 2) containing 0.1% ammonium acetate. The purified blue compound showed absorption peaks at 234, 254, 315, 370, 410, 590 (shoulder) and 633 nm. High-resolution FAB mass spectrometry of this compound indicated a molecular formula of C l C Nai m/z 609.2672 (M - Na + 2H)+, and mlz 631.2524 (M + H)+]. These data, together with the HNMR spectral data, indicated the structure of the blue compound to be 8. 

Using PTLC six major fractions of lipids (phospholipids, free sterols, free fatty acids, triacylglycerols, methyl esters, and sterol esters) were separated from the skin lipids of chicken to smdy the penetration responses of Schistosoma cercaria and Austrobilharzia variglandis [79a]. To determine the structure of nontoxic lipids in lipopolysaccharides of Salmonella typhimurium, monophosphoryl lipids were separated from these lipids using PTLC. The separated fractions were used in FAB-MS to determine [3-hydroxymyristic acid, lauric acid, and 3-hydroxymyristic acids [79b]. 

The unbound PCP concentration was calculated by multiplying the total unchanged PCP concentration In serum by the unbound fraction in serum at each time point. The harmonic means for the terminal elimination half-life for unchanged total PCP and unbound PCP were virtually the same (3.5 and 3.3 hours, respectively). The arrows indicate the time of Fab administration. 

Based on the dramatic changes in volume of distribution and the free fraction of PCP found in serum, we predict that this form of therapy has the potential to rapidly reverse the toxicity of PCP, if sufficient Fab can be administered relative to the dose of PCP, The most practical method for making large quantities of antibodies with reproducible properties is through monoclonal... 

Different options are available for LC-MS instruments. The vacuum system of a mass spectrometer typically will accept liquid flows in the range of 10-20 p,L min-1. For higher flow-rates it is necessary to modify the vacuum system (TSP interface), to remove the solvent before entry into the ion source (MB interface) or to split the effluent of the column (DLI interface). In the latter case only a small fraction (10-20 iLrnin ) of the total effluent is introduced into the ion source, where the mobile phase provides for chemical ionisation of the sample. The currently available commercial LC-MS systems (Table 7.48) differ widely in characteristics mass spectrometer (QMS, QQQ, QITMS, ToF-MS, B, B-QITMS, QToF-MS), mass range m/z 25000), resolution (up to 5000), mass accuracy (at best <5ppm), scan speed (up to 13000Das-1), interface (usually ESP/ISP and APCI, nanospray, PB, CF-FAB). There is no single LC-MS interface and ionisation mode that is readily suitable for all compounds... 

After the sample has entered the gel bed, wash the column with 15ml of lOmM Tris-HCl buffer, pH 8.0, while 2.0ml fractions are collected. Monitor the fractions for protein by their absorbance at 280 nm. The protein eluted unretarded from the column is purified Fab. 

The dissimilar multiprotein complexes, ALP-Fab and ALP-E3-Fab , were similarly purified over an octyl-Sepharose column. The protein fractions eluted from this column were characterized relative to the effective protein concentrations required to generate a specific response equivalent to that of ALP-Fab. These results show (Table 19.4) that the more hydrophobic protein fraction... 

Plasmid DNA (pUC18) Fab fragment from an IgG purified from human sera pH 7.5,30°C Nicked DNA Autoantibodies Human serum IgG fraction (Fab) was found to hydrolyse DNA. Unknown immunogen 4.3 x 101 1.4 x 101 nr 6.5... 

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