Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Forty-eight group A streptococcal strains of different M types were screened for binding of human radiolabeled IgG. Three of the strains bound more than 80% of the added radioactivity and one of them, an M protein type 1 strain designated AP1, was selected for further analysis. Attempts were made to solubilize the IgG binding bacterial molecule, and small amounts of an IgG binding protein with a mol. wt of 40 kDa could be solubilized with mutanolysin, a muramolytic agent. The gene encoding this streptococcal protein was cloned and expressed in E. coli, and the E. coli-produced protein was purified in a single step by affinity chromatography on IgG-Sepharose. When tested with IgGs from different species, the molecule was found to bind human IgG almost exclusively. The N-terminal amino acid sequence was determined and showed no homology with previously isolated Ig binding proteins, and the name protein H (as in human IgG) is suggested for this novel Ig binding bacterial protein. Protein H showed preferential affinity for heavy chains and Fc fragments of human IgG, and did not bind Ig light chains. The affinity constant, determined by Scatchard plots, between protein H and human polyclonal IgG was 1.6 x 10(9). No binding was observed between protein H and IgM, IgA, IgD, or IgE. Finally, when tested against several additional proteins and human plasma, protein H only showed weak binding to alpha 2-macroglobulin, a proteinase inhibitor.
Mol Immunol 1990 Jun
PMID:Protein H--a novel IgG binding bacterial protein. 219 20

Thiopentone-specific IgE antibodies from the sera of subjects who experienced a life-threatening anaphylactic reaction to the drug and IgE antibodies that cross-react with thiopentone via substituted ammonium groups in either cyclic or acyclic form, were studied by direct binding immunoassays and quantitative hapten inhibition methods. Findings provided an explanation for the apparent 'non-specific' nature of some IgE antibody reactions with thiopentone and reinforce the conclusion that the thiopentone IgE immunoassay is a valuable aid in the diagnosis of immediate allergic reactions to the drug.
Mol Immunol 1990 Sep
PMID:The molecular basis of IgE antibody binding to thiopentone. Binding of IgE from thiopentone-allergic and non-allergic subjects. 221 78

Subjects who experience life-threatening anaphylactic reactions to neuromuscular blocking drugs frequently have serum IgE antibodies that react with substituted ammonium groups on the drugs. Failure to detect drug-reactive antibodies may be due to the nature of the drug-solid support used for testing sera. With this in mind, solid phases of some selected compounds containing substituted ammonium groups, in particular triethylamine and morphine, were prepared and used to screen sera in an attempt to increase the frequency of detection of IgE antibodies complementary to tertiary and/or quaternary ammonium groups. For subjects who experienced an anaphylactic reaction to succinylcholine or gallamine, use of the supplementary assays increased the frequency of detection from 83 to 100%. For d-tubocurarine and alcuronium, detections increased from 92 to 100% and from 67 to 88%, respectively. Molecular models revealed a clear structural similarity between the conformations of the trialkylammonium groups on one face of the molecules of morphine and d-tubocurarine.
Mol Immunol 1990 Oct
PMID:Immunoassays employing substituted ammonium compounds other than neuromuscular blocking drugs to increase the detection of IgE antibodies to these drugs. 223 54

A glycoprotein allergen, Art v II, was isolated from pollen of mugwort by two different isolation procedures. Art v II-A was isolated by a combination of ion-exchange chromatography on DEAE-Sepharose, affinity chromatography on Con A-Sepharose and ion-exchange chromatography on Mono P. Art v II-B was isolated by a combination of preparative IEF in Ultrodex granulated gel, affinity chromatography on Con A-Sepharose and HPLC size exclusion on Ultropac TSK G2000SW. Art v II-A and Art v II-B were shown to be antigenically identical with the allergen we have formerly denoted Ag7. The MW of Art v II A/B was determined to be 34,000-38,000 by HPLC size exclusion, and 35,000 and 20,000 by SDS-PAGE under non-reducing and reducing conditions, respectively. Art v II was found to consist of 6(7) isoforms with pI 4.10, 4.20 (major component), 4.35, 4.45, 4.55, 4.65, (4.80). The glycoprotein allergen had a protein to carbohydrate ratio of 10:1 and the carbohydrate part contained mannose (70.7%), N-acetyl-glucosamine (17.0%), glucose (7.0%) and galactose (5.3%). In R(R)IE the purified allergen bound IgE from 5 (33%) of 15 sera from patients with clinical allergy against mugwort pollen and from 13 (52%) of 25 sera from patients selected only on the basis of a RAST-class 4 against mugwort pollen.
Mol Immunol 1990 Oct
PMID:Isolation and characterization of a glycoprotein allergen, Art v II, from pollen of mugwort (Artemisia vulgaris L.). 223 55

Liposomes are non-toxic, biodegradable and feebly immunogenic lipid vesicles made from natural and synthetic lipids. They are known to act as immunopotentiating agents and can be used to formulate sustained release preparation by encapsulation. In the present study, liposome entrapped allergen and free allergen were used to inject in Balb/C mice at different time intervals and their immune response in terms of specific IgG and specific IgE levels was quantitated by ELISA (Enzyme Linked Immuno sorbent Assay). The results indicated that specific IgE response was significantly higher in mice injected free allergen as compared to that of mice given liposome entrapped allergen. However, the specific IgG response was not statistically significant. Experiments carried out with liposome entrapped allergen and liposome coupled allergen showed no statistically significant difference in specific IgE and specific IgG titre between the two groups of mice. This type of immunomodulatory effect of liposomes in reducing IgE levels and without affecting IgG levels may be useful in Type I allergic disorders.
Mol Cell Biochem 1990 Sep 21
PMID:Immunomodulation by liposome entrapped allergen. 228 Jul 64

Immunogenicity of soluble protein antigens in the complexes with synthetic polyions may be regarded as depending both on the nature of polymer carrier and the structure of the protein-polyelectrolyte complex. The immunogenicity of stable soluble complexes of ovalbumin (OA) with polycation - quaternized poly-4-vinylpyridine (C-1) and copolymer of acrylic acid and 2-methyl-5-vinylpyridine (C-2) have been evaluated. Immunization of mice by C-1 have induced a vigorous formation of the anti-OA IgG antibodies and IgE homocytotropic antibodies, while immunogenicity of OA in C-2 was comparable with that of OA alone. The analysis of the structural-chemical features of the complexes investigated has shown that enhanced immunogenicity of C-1 may be due to (1) the non-homogeneous distribution of protein globulae among polycation macromolecules and to (2) the formation of complex with an asymmetrical structure, to (3) the high ability of C-1 to adsorb on a surface of the lymphoid cells and to induce a formation of intercellular aggregates. An enhancing of a stability and a size of C-2 in the presence of Cu2+ shows no influence on a immunogenicity of OA. An immunogenicity of both types of complexes does not depend upon the access of determinants of OA to antibodies so far as it has been shown that complex formation in both cases are not accompanied by an alteration of antigenicity and allergenicity of OA.
Mol Biol (Mosk)
PMID:[The effect of structural-chemical characteristics of water-soluble polyelectrolyte complexes of ovalbumin on their immunological properties]. 236 87

An allergenic protein from Artemisia vulgaris pollen has been purified to homogeneity. Its molecular weight in native conditions is 47,000. The purified allergen, hereafter denominated Art v I, is a monomeric protein. It is a clinically relevant allergen since, at least, 70% of the individuals allergic to Artemisia vulgaris pollen have specific IgE in serum and in mast cells, demonstrated by ELISA and skin prick tests, respectively.
Mol Immunol 1990 Jul
PMID:Purification of Art v I, a relevant allergen of Artemisia vulgaris pollen. 239 37

Allergen molecules from Parietaria judaica pollen, a widely distributed allergy inducer in Southern and Western Europe, have been studied using specific monoclonal antibodies (MAbs). MAbs against IgE-binding components were selected in a 4-step radioimmunoassay. Three different MAbs (AC/1.1, AC/7.1 and AC/15.1) were obtained which recognized epitope(s) located on a polypeptide of 10 Kd (Pj10). This polypeptide displayed the highest IgE-binding ability under either native or SDS-denatured conditions, as determined by immunoadsorption and immunodetection after SDS-PAGE, respectively. The Pj10-containing allergen, purified on an AC/1.1 MAb-Sepharose column, was able to inhibit most of the binding of specific IgE to the pollen extract coupled to paper discs in an inhibition radioallergosorbent test (RAST). The affinity-purified allergen exhibited the same immunoelectrophoretic behaviour as the native allergen.
Mol Immunol 1985 Sep
PMID:Isolation of the major IgE-binding protein from Parietaria judaica pollen using monoclonal antibodies. 241 13

We have previously reported on the production of murine monoclonal antibodies (Mabs) to the retentate fraction of the aqueous extract of Kentucky bluegrass pollen (KBG-R) [Kisil et al. (1980) Fedn Proc. 39, 3479]. In the present study, the ability of one of these Mabs (Mab 12) to recognize various antigenic components present in KBG-R and the corresponding fraction of ryegrass (rye-R) was evaluated by the Western and immunoblot methods. Thus, KBG-R and rye-R were resolved electrophoretically into a large number of components. Remarkably, the concurrent immunoblot analysis with Mab 12 detected only a single antigenic component in each of the retentate fractions. The position of the antigenic component observed on these immunoblots was identical to that obtained with the rye allergen high mol. wt basic antigen (mol. wt 56,800). To characterize the antigenic site recognized by the Mab, the size of HMBA was reduced by cleavage with CNBr, the resulting fragments separated by high-performance liquid chromatography on a reverse-phase column and their antigenic activity analyzed by immunoblot. Two peptides, CB-1 (mol. wt = 17,400) and CB-2 (mol. wt = 22,000), retained the capacity to react with Mab 12 and also IgE antibodies present in a pool of sera from grass allergic individuals.
Mol Immunol 1986 Feb
PMID:Partial characterization of an antigenic site of high molecular weight basic antigen, a ryegrass pollen allergen, using a monoclonal antibody. 242 41

Protamine is an arginine-rich basic polypeptide that stimulates histamine release from rat mast cells but not from human basophils. In this report, we show that protamine causes a non-cytolytic potentiation of IgE-mediated histamine release from human basophils. A direct effect of protamine on basophils was supported by results obtained using cell preparations containing 35-65% basophils. The potentiation occurred at all concentrations of antigen that initiated release and was most pronounced at antigen concentrations that alone stimulated minimal histamine release. The kinetics of potentiated release were parallel to those for IgE-mediated histamine release, and addition of protamine did not overcome the block caused by antigenic desensitization. Staging experiments indicated that enhancement occurred only when protamine and antigen were added together in a single step reaction. Protamine also potentiated release stimulated by eosinophil granule major basic protein or poly-L-lysine, but inhibited release initiated by poly-L-arginine; poly-L-arginine stimulated release was also inhibited by polymyxin B. Arginine-rich histone mimicked the protamine effect, while lysine-rich histone, polymyxin B, and compound 48/80 had minimal or no effect on IgE-mediated release. These results suggest that a polycation recognition site on human basophils similar to that described for rat mast cells may mediate potentiation of basophil secretory events by arginine-rich basic polypeptides.
Mol Immunol 1986 Mar
PMID:Potentiation of human basophil histamine release by protamine: a new role for a polycation recognition site. 242 67


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