Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0393754 (HSA)
 2,996 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In this investigation, the modulating effects of non-immune human IgG and rheumatoid factors (RFs) on antigen-antibody complexations were studied. Non-immune human IgG, as well as RF, were found to inhibit the binding of antigen to specific antibodies of both human and rabbit origin. In addition, human immunoglobulins were also able to modify the composition of preformed antigen-antibody complexes. The effects were detected by immunological methods in two different antigen-antibody systems (human serum albumin-rabbit anti-HSA and tetanus toxoid-human anti-TT). Changes in biological activities could be followed by employing enzymes (glucose-6-phosphate dehydrogenase and human placental alkaline phosphatase) as antigens. The outcome of the effects was found to be dependent on the ratio of antigen to antibody, the antigen-binding properties of the antibody and its origin, and on the properties of the immunoglobulins added. The observed changes could not be explained only by the presence of specific antibodies in the immunoglobulin preparations. The ability of immunoglobulins to modulate antigen-antibody complexations may provide a rationale for the large amounts of non-specific immunoglobulins in the circulation by preventing premature precipitation and promoting the elimination of antigenic molecules.
 ...
PMID:Modulation of antigen-antibody complexations by immunoglobulins. 756 73

A poly(vinyl alcohol) (PVA) coated particulate perfluoropolymer (FEP) support has been functionalised with ion-exchange groups for use in ion-exchange chromatography of proteins. Anion-exchange (DEAE and Q) and cation-exchange (SP) groups were introduced to PVA-FEP which had previously been activated using cyanuric chloride. The equilibrium adsorption capacities of SP-PVA-FEP were 31.8 and 25.2 mg ml-1 for lysozyme and IgG respectively while for DEAE-PVA-FEP, the equilibrium adsorption capacities were 14.9 and 9.7 mg ml-1 for beta-lactoglobulin and HSA respectively. The equilibrium adsorption capacities for Q-PVA-FEP were determined to be 17.2 and 13.5 mg ml-1 for beta-lactoglobulin and HSA respectively. Experiments carried out to investigate the resolving power of materials showed that both SP and Q-PVA-FEP were able to resolve proteins with only small differences in their isoelectric points and that this resolution could be maintained at a flow-rate of 1500 cm h-1. SP-PVA-FEP was used to purify lysozyme from egg whites where a 50-fold purification, to homogeneity, was achieved in 98% yield. The anion exchanger, Q-PVA-FEP could be used to purify G6PDH from a clarified homogenate of bakers' yeast 14.3-fold in 81% yield.
 ...
PMID:Preparation and use of ion-exchange chromatographic supports based on perfluoropolymers. 922 92