Size exclusion chromatography albumin

It is well known that drugs bind to plasma proteins, particularly to serum albumin and a-acid glycoprotein, and that only the unbound, or free, fraction is responsible for any pharmacological effect. For protein-drug binding studies size-exclusion chromatography in one of three variants—namely, the Hum-mel-Dreyer method (1962), the vacancy peak method (Sebille, et al., 1979), and frontal analysis (Cooper and Wood, 1968)—is the traditional method of... 

Ultrafiltration is conducted to remove precipitating agents such as ethanol, PEG, and caprylic acid through diafiltration and to concentrate the protein to the desired level. It has replaced lyophilization for ethanol removal from albumin and immunoglobulins and size exclusion chromatography for buffer exchange. 

Figure 6 Purification of IgM by size exciusion chromatography foliowing euglobulin precipitation. Monoclonal antibody of IgM isotype (MAB 46.3) was purified from ascites by euglobulin precipitation. Precipitated IgM was contaminated by lgG3 and albumin, which were separated further by size exclusion chromatography on a Superose-6 column.

Immobilized antibodies have also been used extensively in multidimensional liquid chromatography (MDLC) analyses. As shown in Fig. 2, an affinity column with immobilized anti-HSA is used to capture all of the human serum albumin in a sample, allowing all of the other components to flow through to waste. Then, the affinity chromatography column is eluted directly into a size-exclusion column where albumin... 

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