Immunochemistry最新文献

{"title":"Binding of immunoglobulins and immune complexes to erythrocytes of vertebrates","authors":"Silvia E. Hajos ,&nbsp;Ricardo A. Margni ,&nbsp;Gabriela Perdigo´n ,&nbsp;Marcela Manghi ,&nbsp;Rodolfo Olivera","doi":"10.1016/0161-5890(78)90034-2","DOIUrl":"10.1016/0161-5890(78)90034-2","url":null,"abstract":"<div><p>Previous investigations which have referred to red cell Fc receptor in rabbit, guinea pig. sheep and man, have been extended to other vertebrates, such as reptiles, amphibia, birds and mammalians.</p><p>In these investigations, red cells from different animal species have been analyzed. As ligand DNP-BSA anti-DNP non-precipitating antibody, aggregated IgG by the bis-diazotized benzidine method. IgM 7S and non-modified IgG, IgA and IgM were used. The ligand binding to red cells was detected by Coombs test with specific anti-immunoglobulin serum.</p><p>The analyzed red cells showed exposed Fc receptor. In the case of human red cells, to render such receptor evident it is necessary to submit the cells to trypsinization.</p><p>All the analyzed erythrocytes bind IgM 7S, Ab-Ag complex and aggregated IgG, and some of these cells bind non-modified immunoglobulins, although none of them bind IgM 19S. These bindings were inhibited by Fcγ, Fcμ and Ag-Ab complex, but they were not inhibited by Fabγ. When specific anti-immunoglobulin serum was added to red cells with bound IgM 7S or Ag-Ab, the clusters which formed by nucleated erythrocytes were bigger than those obtained with non-nucleated red-cells.</p><p>In the case of chicken (nucleated) and sheep (non-nucleated) erythrocytes. the interaction between¹³¹I-IgM_s-red cells at equilibrium showed a similar <em>K</em>₀ for both red cells (chicken <em>K</em>₀ = 1.8 × 10⁸ L/M; sheep <em>K</em>₀ = 1.1 × 10⁸ L/M). The number of Fc receptors by red cell were 1.23 × 10⁶ and 1.21 × 10⁵ for chicken and sheep erythrocytes, respectively. Taking into account these results, the different behaviour of nucleated and non-nucleated red cells with bound IgM 7S, when they react with anti-IgM antibody, would be the consequence of different avidity for both equilibrated systems and not a particular characteristic of their Fc receptors.</p></div>","PeriodicalId":13265,"journal":{"name":"Immunochemistry","volume":"15 9","pages":"Pages 623-628"},"PeriodicalIF":0.0,"publicationDate":"1978-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0161-5890(78)90034-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11938765","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Meeting report: First international symposium on immunobiology of proteins and peptides","authors":"M. Atassi, E. Benjamini, J. Goodman, A. Stavitsky","doi":"10.1016/0161-5890(78)90015-9","DOIUrl":"https://doi.org/10.1016/0161-5890(78)90015-9","url":null,"abstract":"","PeriodicalId":13265,"journal":{"name":"Immunochemistry","volume":"60 1","pages":"603-607"},"PeriodicalIF":0.0,"publicationDate":"1978-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74494281","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Comparison by1H NMR of the hapten environment in the combining site of the dinitrophenyl binding IgA protein 315 and its fragments","authors":"Arabella T. Morris ,&nbsp;David Givol ,&nbsp;Raymond A. Dwek","doi":"10.1016/0161-5890(78)90002-0","DOIUrl":"10.1016/0161-5890(78)90002-0","url":null,"abstract":"<div><p>This paper compares the combining site of the Dnp binding mouse IgA myeloma protein in the Fv and Fab fragments and in the intact IgA. This was done by monitoring the environment of the aromatic hapten protons of DnpO⁻ , Dnp-<span>l</span>-aspartate and Dnp glycine on binding to protein 315, using high resolution 270 MHz¹H NMR. The aromatic Dnp proton resonances undergo large upfield chemical shifts which can be measured directly. These shifts have been interpreted previously as arising from interactions of the hapten with aromatic residues in the combining site. These shifts are an intrinsic reporter of the environment of the hapten in the combining site for each hapten. The magnitudes of the shifts are similar for both the Fv and Fab fragments. The absolute magnitude of the shifts for the IgA could not be measured directly, but the shift ratios for each Dnp proton were found to be similar to those obtained for the Fv and Fab fragments, indicating that the combining site is the same in all three fragments. The line-widths of the bound Dnp proton resonances vary with fragment size and show that the constant regions impose rotational constraints on the combining site. This is in contrast to the rotational freedom of the CH₃ domain which appears to be independent of the rest of the molecule (Burton<em>et al</em>., 1977).</p></div>","PeriodicalId":13265,"journal":{"name":"Immunochemistry","volume":"15 8","pages":"Pages 519-522"},"PeriodicalIF":0.0,"publicationDate":"1978-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0161-5890(78)90002-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11929597","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Antibodies to poly d(A-T) and their reactions with oligonucleotides and nucleic acids","authors":"Beverly W. Lubit ,&nbsp;Bernard F. Erlanger","doi":"10.1016/0161-5890(78)90040-8","DOIUrl":"10.1016/0161-5890(78)90040-8","url":null,"abstract":"<div><p>Antibodies to poly d(A-T)‡ were elicited in two rabbits by immunization with complexes of heat-denatured poly d(A-T) and MBSA. Denaturation of poly d(A-T) was carried out in a salt solution and in distilled water. The antibodies were characterized by precipitation, hemagglutination and radioimmunoassay procedures. The antibody bound poly d(A-T) and cross reactions were observed with dAdo, dThd, poly(b) and ApU but not with UpA.<em>V.faba</em> satellite and calf thymus DNAs were bound at least as well as poly d(A-T); DNA from<em>B. subtilis</em> and<em>Pseudomonas</em> were poorly bound. After absorption of the serum with Ado-RSA, Thd-RSA and BSA, the antisera were directed primarily to heat-denatured poly d(A-T). Cross-reactions were observed with mouse myeloma DNA, poly(dT), poly(dA)-poly(dT) but not with poly(dA). The results indicated that anti-poly d(A-T) recognizes sequence and secondary structures. The immunochemical data are in accord with findings made by other workers on DNA and synthetic polynucleotides by physical studies, such as X-ray diffraction and scattering. Moreover, the immunochemical data support earlier contentions that local conformations in nucleic acids are responsive to primary sequences as is the case with proteins.</p><p>Also described are procedures for the synthesis of poly d(A-T)-[³H]A and poly ([³H]A-T). For the preparation of the latter, TTP was synthesized from TMP which was prepared enzymically from Thd.</p></div>","PeriodicalId":13265,"journal":{"name":"Immunochemistry","volume":"15 9","pages":"Pages 663-671"},"PeriodicalIF":0.0,"publicationDate":"1978-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0161-5890(78)90040-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11938768","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Molecular distribution of allotypic determinants Lpm7 and Lpm8 of mink very high density α2-lipoprotein","authors":"O.K. Baranov,&nbsp;V.I. Yermolaev","doi":"10.1016/0161-5890(78)90035-4","DOIUrl":"https://doi.org/10.1016/0161-5890(78)90035-4","url":null,"abstract":"<div><p>Agar gel double-diffusion experiments demonstrated that the allodeterminants Lpm7 and Lpm8, very high density lipoproteins of mink, reside on different molecules. Molecules possessing Lpm7 and Lpm8 have no other known Lpm-allodeterminants. These results extend our earlier observations on the distribution of Lpm1, Lpm2, Lpm3, Lpm4 and Lpm5 on lipoprotein molecules. It is concluded that Lpm-lipoproteins from mink sera are represented by molecules of several types. identical in their species-specific antigenic properties and each having a unique allodeterminant. The distribution patterns of Lpm7 and Lpm8 among molecules support the suggestion that monogenically inherited allogroups are controlled by closely-linked structural genes.</p></div>","PeriodicalId":13265,"journal":{"name":"Immunochemistry","volume":"15 9","pages":"Pages 629-632"},"PeriodicalIF":0.0,"publicationDate":"1978-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0161-5890(78)90035-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71734371","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Meeting report","authors":"M.Z. Atassi ,&nbsp;E. Benjamini ,&nbsp;J.W. Goodman ,&nbsp;A.B. Stavitsky","doi":"10.1016/0161-5890(78)90015-9","DOIUrl":"https://doi.org/10.1016/0161-5890(78)90015-9","url":null,"abstract":"","PeriodicalId":13265,"journal":{"name":"Immunochemistry","volume":"15 8","pages":"Pages 603-607"},"PeriodicalIF":0.0,"publicationDate":"1978-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0161-5890(78)90015-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"71848859","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Purification, immunochemical and biological characterization of malate dehydrogenase ofSchistosoma mansoni","authors":"D. Bout,&nbsp;H. Dupas,&nbsp;M. Capron,&nbsp;A. El Gazawi ,&nbsp;Y. Carlier,&nbsp;A. Delacourte ,&nbsp;A. Capron","doi":"10.1016/0161-5890(78)90036-6","DOIUrl":"10.1016/0161-5890(78)90036-6","url":null,"abstract":"<div><p>Affinity chromatography with AMP-Sepharose allows us to purify malate dehydrogenase of<em>Schistosoma mansoni</em> and to perform the studies about the immunochemical and biological properties of this enzyme. MDH has a mol. wt 60,000 and has two isoenzymes (pI 7.1 and 8.5), which are antigenically different. Isoenzyme (pI 7.1) is the antigen called 4, specific of the genus<em>Schistosoma</em> and is highly immunogenic. By immunofluorescence, MDH was localized in the cellular layer of the coecum. Mice immunized with purified MDH exhibited a significant decrease of worm burden.</p></div>","PeriodicalId":13265,"journal":{"name":"Immunochemistry","volume":"15 9","pages":"Pages 633-638"},"PeriodicalIF":0.0,"publicationDate":"1978-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0161-5890(78)90036-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11938766","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The alternative complement pathway in bovine serum: The isolation of a serum protein with factor B activity","authors":"A.S.D. Pang,&nbsp;W.P. Aston","doi":"10.1016/0161-5890(78)90004-4","DOIUrl":"10.1016/0161-5890(78)90004-4","url":null,"abstract":"<div><p>A heat labile serum factor (BSF). required for the lysis of unsensitized human erythrocytes by the alternative pathway of bovine complement, has been isolated from bovine serum. The molecular weight of BSF was about 100,000 daltons. A specific antiserum was raised which was able to detect BSF in either serum or in the purified form as a beta-globulin. The antiserum was also used to demonstrate that, in cobra venom factor (CVF) treated bovine sera, the BSF was cleaved into at least two fragments. On the basis of its functional behaviour in haemolytic tests and as an integral component of a CVF-induced C3-convertase activity, BSF appeared to be the bovine counterpart of human factor B.</p></div>","PeriodicalId":13265,"journal":{"name":"Immunochemistry","volume":"15 8","pages":"Pages 529-534"},"PeriodicalIF":0.0,"publicationDate":"1978-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0161-5890(78)90004-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11304562","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"On the structure of the capsular polysaccharide fromCryptococcus neoformans serotype C","authors":"A.K. Bhattacharjee ,&nbsp;K.J. Kwon-Chung ,&nbsp;C.P.J. Glaudemans","doi":"10.1016/0161-5890(78)90041-X","DOIUrl":"10.1016/0161-5890(78)90041-X","url":null,"abstract":"<div><p>The capsular polysaccharide from<em>Cryptococcus neoformans</em> serotype C has been studied using the usual methods for the elucidation of chemical structure. The results are consistent with the occurrence of a polysaccharide having an α 1,3 linked backbone of<span>d</span>-mannopyranoside residues, every other one of which is doubly substituted with two terminal<span>d</span>-xylopyranosyl residues linked β (1,2 and β 1,4 respectively, and with the remainder of the mannosyl residues substituted with a terminal<span>d</span>-glucuronosidopyranosyl residue linked β 1,2. Alternatively, the terminal glucuronic acid residue may be β (1,2 linked to a mannosyl residue in the chain already hearing a singly branched β 1,4 xylopyranosyl residue, while the neighboring mannosyl residue carries a single branch of β 1.2 xylopyranoside.</p></div>","PeriodicalId":13265,"journal":{"name":"Immunochemistry","volume":"15 9","pages":"Pages 673-679"},"PeriodicalIF":0.0,"publicationDate":"1978-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0161-5890(78)90041-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10828978","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Further studies of an anomalous cross-reaction involving worm and vertebrate lysozymes","authors":"Ellen M. Prager ,&nbsp;Allan C. Wilson ,&nbsp;Jean-Pierre Pe´rin ,&nbsp;Pierre Jolle`s","doi":"10.1016/0161-5890(78)90011-1","DOIUrl":"10.1016/0161-5890(78)90011-1","url":null,"abstract":"<div><p>Lysozyme was purified from the annelid worm<em>Nephthys hombergii</em> and re-examined for immunological cross-reactivity with antisera to human and chicken lysozymes. It was determined that the previously reported reaction between worm lysozyme and anti-human lysozyme and also the presently observed reaction between worm lysozyme and anti-chicken lysozyme were due to the presence of small amounts of vertebrate-like<em>c</em>-type lysozymes in the worm enzyme preparations. The cross-reactions were not attributable to the major lysozyme component in the worm preparations.</p></div>","PeriodicalId":13265,"journal":{"name":"Immunochemistry","volume":"15 8","pages":"Pages 577-583"},"PeriodicalIF":0.0,"publicationDate":"1978-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0161-5890(78)90011-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11323785","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}