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1.
Clin Chem ; 33(9): 1543-7, 1987 Sep.
Article in English | MEDLINE | ID: mdl-3113767

ABSTRACT

We have used chromium dioxide magnetic particles as the solid support in developing a series of immunological tests. The high surface area (greater than 40 m2/g) available on the magnetic particles and their easy dispersion throughout a solution allow for rapid and complete capture of the target antigen. The magnetic responsiveness of the particles allows for rapid, high-efficiency washing to reduce nonspecific binding, which often limits the sensitivity of serological assays. These features form the basis of extremely rapid and flexible assays for several hormones and markers of cancer and infectious disease. Most of the assays involve monoclonal antibodies. Here we describe specific performance characteristics for thyroxin, follitropin, creatine kinase isoenzyme MB, and antibody to human immunodeficiency virus (HIV). All of the assays are performed in less than 90 min, many in 30 to 45 min. The technology is highly flexible and is suitable for a variety of formats, from manual to fully automated.


Subject(s)
Chromium Compounds , Chromium , Immunoassay/methods , Alkaline Phosphatase , Antibodies, Monoclonal , Antibodies, Viral/analysis , Creatine Kinase/analysis , Follicle Stimulating Hormone/analysis , HIV/immunology , Humans , Indicators and Reagents , Isoenzymes , Magnetics , Thyroxine/analysis
3.
J Immunol Methods ; 44(3): 271-84, 1981.
Article in English | MEDLINE | ID: mdl-7276580

ABSTRACT

The relative affinities of an antibody population of different antigens or of different antibody populations for one antigen can be determined by quantitative immunoelectrophoresis. Antigen-antibody interactions of greater average affinity result in a greater increase in rocket area as a function of the amount of antigen applied to the wells. This is measured as the slope of the line in plots of rocket area versus antigen amount. Quantitative immunoelectrophoresis of different antigens, which nevertheless have the same affinity for antibody, produces plots with the same slopes. The relative magnitudes of the slopes of these lines reflect the relative average affinities of different antibody populations for an antigen.


Subject(s)
Antibody Affinity , Antigens/immunology , Animals , Antibody Specificity , Cross Reactions , Goats , Hemoglobin A , Hemoglobin A2 , Humans , Immunoelectrophoresis , Rabbits
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