Competitive Protein Adsorption of Albumin and Immunoglobulin G from Human Serum onto Polymer Surfaces

Abstract We describe a simple method for detecting enzyme--immunoglobulin G (IgG) complexes in human serum. Protein-A Sepharose CL-4B binds IgG and therefore also the enzyme--IgG complexes, which can then be separated easily from the serum by centrifugation. We demonstrate this separation in two patients, one with a complex of IgG and creatine kinase (EC 2.7.3.2) BB isoenzyme, the other with an IgG--alkaline phosphatase (EC 3.1.3.1) complex. Both patients had unexplainably high activities of the respective enzymes in their serum. The method we propose should be a useful, simple, routine method of detection in cases where IgG--enzyme complexes are suspected.

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Comparative whole corona fingerprinting and protein adsorption thermodynamics of PLGA and PCL nanoparticles in human serum

Colloids and Surfaces B Biointerfaces ◽

10.1016/j.colsurfb.2020.110816 ◽

2020 ◽

Vol 188 ◽

pp. 110816 ◽

Cited By ~ 1

Author(s):

Myolisi Ndumiso ◽

Nela Buchtová ◽

Lizex Husselmann ◽

Gadija Mohamed ◽

Ashwil Klein ◽

...

Keyword(s):

Human Serum ◽

Protein Adsorption ◽

Adsorption Thermodynamics

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Autoantibodies to thyroxin and triiodothyronine in the immunoglobulin G fraction of serum.

Clinical Chemistry ◽

10.1093/clinchem/34.12.2561 ◽

1988 ◽

Vol 34 (12) ◽

pp. 2561-2562 ◽

Cited By ~ 8

Author(s):

L Li Calzi ◽

S Benvenga ◽

S Battiato ◽

F Santini ◽

F Trimarchi

Keyword(s):

Thyroid Hormone ◽

Thyroid Hormones ◽

Human Serum ◽

Immunoglobulin G ◽

Subacute Thyroiditis ◽

Total Serum ◽

Graves Disease ◽

Carrier Proteins ◽

Weak Binding ◽

Idiopathic Myxedema

Abstract Thyroid hormone antibodies (THAbs)--i.e., antibodies to thyroxin (T4) and triiodothyronine (T3)--are detected rarely in human serum, where they are searched for, possibly because of a quantitatively minimal interaction between thyroid hormones (the haptens) and serum IgGs (the antibodies). The weak binding could result from these facts: (a) there are already six physiological carrier proteins for thyroid hormones; (b) THAbs usually account for a very small fraction of the total serum IgGs; (c) THAbs may have--as reported in the literature--a relatively low affinity. To ascertain whether THAbs could pass undetected in serum, we measured antibodies to T3 and T4 in both the serum and the corresponding IgG fraction of six normal persons and 45 patients with various thyroid diseases (Graves' disease, idiopathic myxedema, Hashimoto's thyroiditis, subacute thyroiditis, tumors), using radioimmunoprecipitation. The prevalence of antibodies to T4 was 0/51 in both the sera and the IgG fractions; the prevalence of antibodies to T3 was 1/51 in both materials. Because all of the sera that tested THAb negative were confirmed to be so in the THAb assay of the IgG fraction, we conclude that the prevalence of serum THAbs is not underestimated and that autoimmunization against thyroid hormones is really a rare phenomenon.

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