Chromatography immunoadsorption

Immunoadsorption of rabbit anti-haemocyanin for subsequent cross-linking and use in immunoaffinity chromatography (immunoadsorption)... 

Isolation of prolactin by immunoadsorption Isolation of a pseudo-Tamm-Horsfall glycoprotein by affinity chromatography Isolation of a pseudo-Tamm-Horsfall glycoprotein by affinity chromatography Immunoadsorption of anti-(blood-group A substance) antibody... 

ApoD is found in association with LCAT and with apoA-I in the HDL fraction. Albers et al. used a specific antibody to apoD to remove all apoD by immunoadsorption chromatography from plasma about 64% of LCAT activity and 11% of apoA-I were also removed from plasma (A14). Purified apoD has an apparent Mr of 32,500, and appears as three isoforms on isoelectric focusing (pi 5.20, 5.08, and 5.00) (A14). An HDL apolipoprotein, Mr 35,000, has been thought to be apoD, and to be a cholesteryl ester transfer protein (i.e., to transfer newly synthesized esterified cholesterol from HDL to LDL) (C8). Cholesteryl ester transfer activity in plasma was removed by polyclonal immunoglobulin to apoD (C8, F10). However, Morton and Zilversmit (M41) were able to separate apoD and lipid transfer protein (i.e., the cholesteryl ester transfer protein, or lipid transfer protein I) by chromatography, and they showed that the removal of apoD from plasma by precipitation with specific antisera did not remove any lipid transfer activity. Albers et al. (A14) also showed that immunoadsorption with antibody specific for apoD removed all the apoD from plasma without removing any cholesteryl ester transfer activity. 

An amylase, previously detected in barley and described as a new barley amylase, has been further purified by immunoadsorption and ion-exchange chromatography. Analysis by isoelectric focusing and immunochemical techniques showed that the enzyme preparation did not contain the normal a-and 8-amylases usually found in barley and malt. The enzyme had a very low isoelectric point ca. pH 3.0) and was identified as an a-amylase on the basis of its action pattern on amylose. 

Two forms of a-D-mannosidase from yellow wax beans Phaseolus vulgaris) have been purified by immunoadsorption. A high degree of immunological identity has been demonstrated between a-D-mannosidase I and II from P. vulgaris. This made possible the purification of both forms of the enzyme by chromatography on an immunoadsorbent prepared from anti-fa-D-mannosidase I) antiserum. 

Considerable effort continues to be devoted to the development of new methods of enzyme immobilization and of novel affinity chromatography media. Immunoadsorption has been applied to the isolation of numerous biologically important molecules. Oligosaccharides co-polymerized with acrylamide have been exploited with much success for the isolation of many lectins from different sources. Active immobilized cells have been prepared and their potential applications for industrial processes and in medicine have been demonstrated. 

Polysaccharide carriers have been widely used for the preparation of immuno-adsorbents. Techniques and instrumentation for preparative immunoadsorptive separations have been discussed. The application of reversed immunosorbents to the immobilization of specific antibodies has been outlined, and a review of the use of affinity chromatography for the isolation of im-munologically reactive cells has appeared. ... 

Purification of specific anti-(2,4-dinitrophenyl) antibodies by immunoadsorption Purification of Datura stramonium phytohaemagglutinin by affinity chromatography Affinity chromatography of Phaseolus vulgaris phytohaemaglutinin... 

Purification of oestradiol receptor of calf uterus by affinity chromatography Purification of collagenase by affinity chromatography isolation of anti-haptoglobin antibodies by immunoadsorption Removal of interspecies reactivity from anti-(immunoglobulin G) sera (human or rabbit) Investigation of the properties of the immobilized IgG... 

Purification of detergent-solubilized la antigens Isolation of a-o-mannosidase from jack bean by affinity chromatography Preparation of specific anti-(unc 54-myosin) antibodies by immunoadsorption Affinity chromatography of glycosidases... 

Purification by affinity chromatography of membrane receptors for Pal and Pa2 Purification of anti-(picryl T suppressor factor) antibody by immunoadsorption Purification of retinol-binding protein by affinity chromatography... 

The repeated use of derivatives of agarose cyclic imidocarbonate in affinity chromatography has been discussed from the viewpoints of the nature of the binding of the protein to the affinant and the methods for regenerating used columns, etc. Agarose cyclic imidocarbonate has been used in automated immunoadsorption and affinity chromatographies. ... 

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