Immunochemical properties of trypsin fragments of human thyroglobulin

1980 ◽  
Vol 94 (2) ◽  
pp. 188-195 ◽  
Author(s):  
R. Dominici ◽  
G. B. Salabé ◽  
A. Diodato ◽  
M. Sorcini ◽  
M. G. di Iorio ◽  
...  
Keyword(s):  
Gel Filtration ◽  
Rabbit Antiserum ◽  
Antigenic Determinants ◽  
Good Activity ◽  
Autoimmune Process ◽  
Autoimmune Thyroid Diseases ◽  
Autoimmune Thyroid ◽  
Tryptic Digest ◽  
Antigenic Activity ◽  
Antigenic Properties

Abstract. Purified human thyroglobulin (Tg) was enzymatically digested with trypsin. After completion of digestion, the tryptic digest was fractionated by gel filtration on a Biogel A 1.5 m column. Further separation and isolation of the major peak C was carried out on a Sephadex G-75 column. Nine fractions were separated and antigenic properties evaluated by a specific and sensitive radioimmunoassay using a rabbit antiserum to 19S Tg and three different antisera from patients with autoimmune thyroid diseases. The Tg fragments react with both hetero- and auto-antisera. The highest antigenic activity was found on larger fragments, but a fairly good activity was also observed on fragments (C6, C7) with lower molecular weight. Antigenic determinants of Tg differ in individual sera suggesting that different sets of determinants elicit the autoimmune process.

scholarly journals Cleavage of bacterial flagellin with cyanogen bromide. Antigenic properties of the protein fragments

1969 ◽  
Vol 113 (3) ◽  
pp. 501-506 ◽  
Author(s):  
C. R. Parish ◽  
R. Wistar ◽  
G. L. Ada
Keyword(s):  
Cyanogen Bromide ◽  
Antigenic Determinants ◽  
Protein Fragments ◽  
Antigenic Activity ◽  
Antigenic Properties ◽  
Bacterial Immobilization ◽  
Test Fragment

1. Four polypeptide fragments, obtained by cyanogen bromide treatment of the protein flagellin from Salmonella adelaide, were tested for their antigenic activity by using them as inhibitors in three different assays: bacterial immobilization, haemagglutination of sensitized erythrocytes and quantitative micro precipitation. Immunodiffusion studies were also performed on the protein fragments. 2. Cleavage of the flagellin molecule in this way gave no detectable loss of antigenic determinants. Fragment A (mol.wt. 18000), the largest of the polypeptides, contained all the antigenic specificities present on flagellin that were recognized by the antisera used. In one test, fragment B (mol.wt. 12000) also contained antigenic activity to an extent not easily explainable by contamination with fragment A. Fragments C (mol.wt. 5500) and D (mol.wt. 4500) appeared to be antigenically inactive.

Antigenic Properties Of Human Fibrin Plasmic Fragment D-Dimer And Its γ-γ Chain Remnant

1981 ◽  
Author(s):  
C S Cierniewski ◽  
P Nowak ◽  
T Krajewski
Keyword(s):  
Ion Exchange ◽  
Competitive Inhibition ◽  
Degradation Products ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Antigenic Determinants ◽  
Human Fibrinogen ◽  
Antigenic Properties ◽  
D Dimer

Immunochemical analyses of human D-dimer and its γ-γ chain remnant were performed to identify their antigenic markers which would be of value in distinguishing between disseminated intravascular coagulation and primary fibrinogenolysis. Cross-linked fibrin was obtained by direct clotting of the fresh citrated plasma after adding excess CaCl2. The plasmic digests of the cross-linked fibrin were fractionated by ion-exchange chromatography and gel filtration. Thus, high molecular weight D-dimer was purified. The γ-γ peptide remnant was purified by ion-exchange chromatography on CM-52 cellulose from the reduced D- dimer. Purity of both polypeptide fragments was determined by standard techniques. They were used to immunize rabbits. Antisera to D-dimer and γ-γ chain remnant were characterized in binding assays and in equilibrium competitive inhibition assays in order to analyze the expression of their antigenic determinants in intact fibrinogen and its plasmic degradation products. Antisera to D-dimer preferentially bound D-dimer and γ-γ chain remnant and to a lesser extent fragment D and fibrinogen. Similarly, antisera to γ-γ chain remnant bound mostly γ-γ , D-dimer as well as γ poiypeptide chain. There was no binding of the intact human fibrinogen. The results obtained in the competitive inhibition assays employing antisera to D-dimer and γ-γ chain remnant, before and after adsorption with fragment D or γ polypeptide chain respectively, as well as fibrin fragments are discussed in this report.

The role of components of Bifidobacterium and Lactobacillus in pathogenesis and serologic diagnosis of autoimmune thyroid diseases

2011 ◽  
Vol 2 (2) ◽  
pp. 139-154 ◽  
Author(s):  
E. Kiseleva ◽  
K. Mikhailopulo ◽  
O. Sviridov ◽  
G. Novik ◽  
Y. Knirel ◽  
...  
Keyword(s):  
Molecular Mechanisms ◽  
Molecular Mimicry ◽  
Thyroid Diseases ◽  
Whole Body ◽  
Thyroid Peroxidase ◽  
Autoimmune Thyroid Diseases ◽  
Bifidobacterium Adolescentis ◽  
Autoimmune Thyroid ◽  
Antigenic Properties

During recent years, researchers have been focusing on the concept of an infectious etiology of autoimmune diseases. The most discussed theory is molecular mimicry, i.e. the emergence of autoreactive clones of T- and B-lymphocytes as a result of cross-immune response to homologous bacterial or viral antigen. Information on the role of probiotic microorganisms (PM) in the molecular mechanisms of autoimmune thyroid diseases (ATD) is limited. Using proteins and immunogenic peptides databanks and relevant computer programs, the homology between the amino acid sequences of thyroid peroxidase (TPO) and thyroglobulin (Tg), which are potential B- and T-cell epitopes of these antigens, and proteins of bifidobacteria and lactobacilli was established. Moreover, we have found components of cells of Bifidobacterium bifidum 791, Bifidobacterium adolescentis 94 BIM, Bifidobacterium longum B379M and Lactobacillus plantarum B-01 that selectively bind human antibodies to TPO (anti-TPO) and antibodies to Tg (anti-Tg) and compete with natural antigens for the binding of anti-TPO and anti-Tg in ELISA. Additionally, a three-fold difference was observed between the probability of detecting antibodies (Abs) to the antigens of L. plantarum B-01 and B. bifidum 791 in serum samples containing and those not containing anti-TPO. On the whole, our data are arguments in favour of the assumption of the possible role of PM of the genera Bifidobacterium and Lactobacillus in triggering ATD by the mechanism of molecular mimicry. The data obtained in silico and in vitro should be proven by use of animal models and clinical studies for extrapolations to the whole body. Possible antigenic properties of components/proteins of bifidobacteria and lactobacilli, selectively binding anti-TPO and anti-Tg should be taken into consideration. Natural human Abs to these bacterial components are probably able to cross-react with the TPO and Tg in the ELISA for detection of anti-TPO and anti-Tg, which are serologic markers of ATD. It can lead to unspecific false positive results and, hence, to an incorrect diagnosis.

Analysis of chosen polymorphisms in FoxP3 gene in children and adolescents with autoimmune thyroid diseases

2014 ◽  
Author(s):  
Artur Bossowski ◽  
Hanna Borysewicz-Sanczyk ◽  
Natalia Wawrusiewicz-Kurylonek ◽  
Mieczyslaw Szalecki ◽  
Beata Wikiera ◽  
...  
Keyword(s):  
Children And Adolescents ◽  
Thyroid Diseases ◽  
Autoimmune Thyroid Diseases ◽  
Foxp3 Gene ◽  
Autoimmune Thyroid

Synthesis of hepatitis B surface antigen pre-S2 region fragments and studies on their immunogenicity

1988 ◽  
Vol 53 (11) ◽  
pp. 2952-2956 ◽  
Author(s):  
Bernard Lammek ◽  
Zbigniew Maćkiewicz ◽  
Izabela Derdowska ◽  
Hanna Świderska ◽  
Adam Nowosławski ◽  
...  
Keyword(s):  
Hepatitis B ◽  
Surface Antigen ◽  
Solid Phase ◽  
Hepatitis B Surface Antigen ◽  
Gel Filtration ◽  
Exchange Chromatography ◽  
Antigenic Determinants ◽  
Phase Method ◽  
Peptide Fragments ◽  
Humoral Immune

Two peptide fragments of hepatitis B surface antigen pre-S2 region were synthesized by the solid phase method. The peptides were purified by gel filtration or ion-exchange chromatography on Sephadex SP-C-25. Both peptides induced a cellular and humoral immune response in rabbits. The results showed that fragment 14-22 of pre-S2 region contains one of the antigenic determinants.

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