Goat Immunoglobulin Research Articles

Radioimmunoassay of murine leukemia virus p30 using staphylococcus aureus as immunoadsorbent

A competition radioimmunoassay for murine leukemia virus p30 has been developed. Serial dilutions of the unknown in wells of microtiter plates are incubated with 125I-labeled p30 and goat antiserum specific for p30. Bound p30 is then removed by an immunoadsorbent specific for goat immunoglobulin, prepared from S. aureus. An internal standard of 51Cr is used to correct for volumetric errors, the amount of the labeled p30 precipitated being calculated from the 125I/51Cr ratio of the supernatant. The assay is rapid, being completed within 2 h, precise, having a coefficient of variation less than 1%, and sensitive, being capable of detecting p30 concentrations as low as 2 ng/ml in a volume of 0.02 ml. It has been used to measure p30 levels in a series of MCA-induced fibrosarcomas of BALB/c mice.

Particle counting immunoassay (Pacia). I. A general method for the determination of antibodies, antigens, and haptens

By using a device designed for counting blood cells, it is possible to measure the agglutination of polystyrene beads (0.8 μ) with accuracy and great sensitivity, the agglutination resulting in a reduction in the number of particles. The latter coated with antigen can be used for determining IgM or IgG antibodies e.g. human rheumatoid factor or rabbit anti-bovine serum albumin antibodies. Macromolecules with multiple antigenic determinants agglutinate particles carrying specific antibodies. This system has been applied for determining HPL and α 1-fetoprotein with a threshold of sensitivity of about 10 μg/l. However the agglutination was decreased by serum factors which led to a 10-fold loss of sensitivity. The interference of rheumatoid factor which agglutinated the particles coated with rabbit or goat immunoglobulins could be avoided by reduction of the serum to be analyzed with 5 mM dithiothreitol for 5 min. Haptens, i.e. DNP-lysine and T 4, were determined by their inhibitory activities toward their specific antibodies, the agglutinator being a hapten-macromolecule conjugate or the antibodies themselves.

Reaction of selenium with immunoglobulin molecules

Radioactive selenite reacts with purified human and goat immunoglobulins at acidic and neutral pH. The antigenic properties of the immunoglobulins are retained during the selenium labelling as shown by immunoelectrophoresis and autoradiography. Pepsin digests of 75Se-labelled IgG possess 75Se both in the (Fab′) 2 fraction and in the low molecular weight peptides derived from the Fc domains. Alpha-l-acid glycoprotein, ribonuclease, and lysozyme are also labelled by this procedure. Enhancement of 75Se incorporation by urea, guanidinium chloride, mercaptoethanol, sodium sulfite and carrier selenite is interpreted as an effect of destabilization of IgG disulfide bonds. Up to 1.4g atoms Se per mol IgG have been incorporated. We assume that selenite is cleaving disulfides by a process akin to sulfitolysis. The lability of the isolated 75Se-labelled IgG to high concentrations of mercaptans and sulfite is consistent with this idea. These 75Se-labelled proteins may be useful in structure studies and radioimmunoassay.

The Solubility of Insect Juvenile Hormone in Aqueous Solutions and Its Adsorption by Glassware and Plastics

Abstract The C18 juvenile hormone of insects can be dissolved in aqueous solutions up to a concentration of 2.5 - 3.0 × 10-5 M; changes in pH, buffer composition and ionic strength hardly affect this solu­bility. The hormone is salted out gradually by increasing ammonium sulphate concentrations. The juvenile hormone is bound to proteins such as bovine serum albumin or goat immunoglobulin G and can be kept in solution by these proteins up to 10-3 M. The hormone is strongly absorbed by many commonly used plastic materials but only to a lesser extent by glass and teflon.

Investigation of the antigenicity of the carbohydrate moiety of chicken ovalbumin

Evidence for the antigenicity of the carbohydrae moiety of ovalbumins was sought by methods capable of detecting specific antibodies. These methods include: (a) the immunoelectrophoretic reaction of the ovalbumins with IgG fraction of goat antichicken ovalbumin serum in the presence and absence of Concanavalin A, (b) the ability of 14C-acetylglycopeptides from chicken ovalbumin to be coprecipitated with the goat immunoglobulins, using the Farr technique, and (c) the ability of the 14C-acetylglycopeptides to be coprecipitated with the goat immunoglobulins, using rabbit antigoat IgG. In no instance was there any evidence for the presence of carbohydrate-specific antibodies. The data strongly suggest that the carbohydrate moiety of chicken ovalbumin is not antigenic in the goat. The failure to detect specific antibodies in goat antiovalbumin IgG is discussed in relation to availability of the carbohydrate moiety for reaction with antibody, to alteration of the carbohydrate's conformation in the glycopeptides relative to its conformation in native ovalbumin, and in relation to the role of the carbohydrate moiety in the phylogeny of avian ovalbumins.

Basement membrane in hepatic coccidiosis of the rabbit

The changes of the basement membrane of intrahepatic bile ducts in the evolution and regression of the papillomatous reaction induced by Eimeria stiedae were studied on 40 young rabbits using a histological and immunofluorescent methods. The results showed that a PAS-positive basement membrane could be demonstrated in the early stages of the papillomatous transformation and that its thickness increased remarkably in the fully developed stage of papillomatous evolution which paralleled the active stage of gametogony. The membrane usually remained thickened throughout the course of epithelial regression and regeneration. There was a localization of fluoro-conjugated goat and anti-rabbit globulin immunoglobulin in the thickened basement membranes beginning at the early stage of gametogony. This evidence suggests that progressive thickening of the basement membranes of the infected bile ducts was mainly aimed at supporting the hyperplastic papillary epithelium and the altered basement membrane after degeneration and/or necrosis of the infected papillary epithelium in the stage of regression assisted the orientation of the newly formed epithelial cells in the process of healing. There is no convincing evidence that a thickened basement membrane or a deposition of globulin as such could strengthen the local defence mechanism to any significant extent.

Interchain disulfide bonds of goat immunoglobulin G.

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTInterchain disulfide bonds of goat immunoglobulin GP. H. Strausbauch, E. Hurwitz, and D. GivolCite this: Biochemistry 1971, 10, 12, 2231–2237Publication Date (Print):June 8, 1971Publication History Published online1 May 2002Published inissue 8 June 1971https://doi.org/10.1021/bi00788a008RIGHTS & PERMISSIONSArticle Views136Altmetric-Citations12LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit PDF (1 MB) Get e-Alerts Get e-Alerts

Identification of secretory IgA, free secretory piece and serum IgA in the ovine and caprine species

Caprine and ovine IgA were identified by cross-reaction with anti-human and anti-bovine IgA sera in colostrum, mature milk, saliva, urine and serum. Secretory component (SC) was shown in the free form and associated with polymeric serum IgA in secretions. Mean molecular weights were determined for the IgA and the free secretory components. The high IgA content of saliva suggested that it was a major secretory immunoglobulin in these species. Traces of secretory IgA were also found in normal sera but most of the serum IgA had no secretory determinant. Secretory IgA, serum IgA and free secretory component were purified. Levels of the sheep and goat immunoglobulins were measured in various fluids.

Goat immunolobulin G. Peptide chains and terminal residues.

Goat immunoglobulin G (IgG) was isolated and characterized. The molecular weights of the IgG and its heavy chains and light chains were found to be 144000, 53600 and 23000 respectively. The light chain corresponds to human L type as was shown by the absence of C-terminal S-carboxymethylcysteine and its high content of N-terminal pyrrolid-2-one-5-carboxylic acid (PCA). The major C-terminal residue of the light chain was serine and the major N-terminal dipeptide was PCA-Ala (0.6mole/mole). The major C-terminal residue of the heavy chain was glycine and the N-terminal sequence of the heavy chain is PCA-Val-Gln. This tripeptide was obtained in a 70% yield.