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1.
Biol Pharm Bull ; 31(3): 507-10, 2008 Mar.
Article in English | MEDLINE | ID: mdl-18310919

ABSTRACT

Biotin-binding IgG (B-IgG) in human sera was quantified using previously developed F(ab')(2)anti-human IgG-coated multiwell microplates (Muratsugu M. et al., 2003, Biol. Pharm. Bull., 26, 1605--1608). The levels of B-IgG in sera, however, were higher than those we predicted. In this study, we modified the assay using F(ab')2anti-human IgG-coated multiwell microplates and successfully quantified the levels of B-IgG in sera. The cause of the unpredicted results was discussed in the text. In addition, the levels of biotin-binding IgA (B-IgA) and IgM (B-IgM) in sera could be measured using F(ab')2anti-human IgA- or IgM-coated multiwell microplates. We quantified B-IgG, B-IgA, and B-IgM in sera from healthy specimens and patients with bronchial asthma, atopic dermatitis, epilepsy, and juvenile rheumatoid arthritis.


Subject(s)
Carrier Proteins/blood , Immunoglobulin A/blood , Immunoglobulin Fab Fragments , Immunoglobulin G/blood , Immunoglobulin M/blood , Receptors, Immunologic/immunology , Biotinylation , Carrier Proteins/immunology , Humans , Immunoassay/methods , Immunoglobulin Fab Fragments/immunology , Reference Standards
2.
Biosens Bioelectron ; 22(11): 2598-603, 2007 May 15.
Article in English | MEDLINE | ID: mdl-17118644

ABSTRACT

Plasma-polymerized films were formed on flat glass plates using allylamine, acrylic acid, acrolein, and allylcyanide as monomers. Adsorption of (125)I-labeled-proteins such as immunoglobulin G (IgG), its F(ab')(2) and Fc fragments, and human serum albumin (HSA) was measured on these plasma-polymerized (PP) films covering the glass plates and on commercially available polymer plates. The adsorption isotherm followed the Langmuir equation, from which the binding constant and amount of saturation binding were estimated. We found that, in general, a cationic surface had higher affinity for protein adsorption than an anionic surface. Among the surfaces examined, the PP-allylamine surface showed the highest binding capacity (264.2 nmol/m(2)) for F(ab')(2) fragment: it was remarkably high. Of the surfaces examined, the PP-acrylic acid surface showed the lowest binding capacity (12.8 nmol/m(2)) for F(ab')(2) fragment. The PP-acrylic acid surface also indicated the lowest protein binding capacity for IgG (16.5 nmol/m(2)), Fc-IgG (32.4 nmol/m(2)) and HSA (16.7 nmol/m(2)), respectively. These imply that the PP-acrylic acid film is useful to fabricate as a low protein adsorption material which expected to decrease cell adhesion. Results of our investigation indicate that the plasma-polymerization technique is promising for fabrication of a smart NanoBio-interface which can control the protein adsorption on a solid-phase substrate using a suitable monomer such as allylamine for the large adsorption and acrylic acid for the small adsorption.


Subject(s)
Allylamine/chemistry , Coated Materials, Biocompatible/chemistry , Immunoglobulin Fc Fragments/chemistry , Immunoglobulin G/chemistry , Iodine Radioisotopes/chemistry , Polymers/chemistry , Radioimmunoassay/methods , Adsorption , Binding Sites , Biosensing Techniques/methods , Gases/chemistry , Hot Temperature , Isotope Labeling/methods , Materials Testing , Membranes, Artificial , Protein Binding
3.
Biol Pharm Bull ; 29(7): 1480-2, 2006 Jul.
Article in English | MEDLINE | ID: mdl-16819193

ABSTRACT

Biotin-binding IgG in human sera was quantitated using F(ab')(2)anti-human IgG-coated multiwell microplates (Muratsugu, M. et al. 2003, Biol. Pharm. Bull., 26, 1605-1608). The biotin-protein ratio of biotinylated IgG, which was used as standard in the assay, was very important to quantitate the level of biotin-binding IgG. We investigated a synthesis method of biotinylated human immunoglobulins, how to determine the biotin-protein ratio of the biotinylated proteins, and their stability to prepare standards for measuring biotin-binding IgG, IgA, and IgM.


Subject(s)
Biotin/pharmacokinetics , Immunoglobulins/chemistry , Biotinylation , Humans , Immunoglobulin A/metabolism , Immunoglobulin G/metabolism , Immunoglobulin M/metabolism , Protein Binding , Serum Albumin, Bovine/metabolism
4.
Biol Pharm Bull ; 26(11): 1605-8, 2003 Nov.
Article in English | MEDLINE | ID: mdl-14600410

ABSTRACT

Biotin-binding human immunoglobulin G (B-IgG) was quantitatively measured using an F(ab')2anti-human IgG-coated multi-well microplate for the first time. B-IgG was caught by F(ab')2anti-human IgG and was detected by the following detecting reagents: Peroxidase-labeled streptavidin, avidin and peroxidase-biotin, or avidin-biotinylated peroxidase complex with method A, B, or C, respectively. Commercially available B-IgG was detected by all these three methods. However, method A and B could not detect B-IgG in the human sera used in this study, but we quantitatively measured the B-IgG level using method C. The result is probably due to the fact that the sensitivity of method C was higher than that of methods A or B. Properties of B-IgG detected by method C are discussed in the text.


Subject(s)
Binding Sites, Antibody , Biotin/blood , Immunoglobulin G/blood , Receptors, Immunologic/blood , Dose-Response Relationship, Immunologic , Humans , Protein Binding/immunology
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