Immunochemistry最新文献

Induction of anti-phosphorylcholine antibodies of restricted heterogeneity in rabbits 兔体内有限异质性抗磷胆碱抗体的诱导

Immunochemistry Pub Date : 1978-12-01 DOI: 10.1016/0161-5890(78)90120-7

Bernard Vray , Johan Hoebeke , Remi Zeeuws , A. Donny Strosberg

引用次数: 2

The effect of immune complex composition on complement activation and complement dependent complex release 免疫复合物组成对补体激活和补体依赖性复合物释放的影响

Immunochemistry Pub Date : 1978-12-01 DOI: 10.1016/0161-5890(78)90123-2

Eva Rajnavo¨lgyi , G. Fu¨st , Judit Kulics , Julia Ember , G.A. Medgyesi , J. Gergely

引用次数: 14

Precise determination of the entire antigenic structure of lysozyme: Molecular features of protein antigenic structures and potential of ‘surface-simulation’ synthesis—a powerful new concept for protein binding sites 精确测定溶菌酶的整个抗原结构:蛋白质抗原结构的分子特征和“表面模拟”合成的潜力-蛋白质结合位点的强大新概念

Immunochemistry Pub Date : 1978-12-01 DOI: 10.1016/0161-5890(78)90126-8

M. Zouhair Atassi

引用次数: 207

Preparation of an active Fd fragment by cyanogen bromide cleavage of an IgG heavy chain from a homogeneous rabbit antibody 溴化氰裂解兔抗体IgG重链制备活性Fd片段

Immunochemistry Pub Date : 1978-12-01 DOI: 10.1016/0161-5890(78)90127-X

P.H. Ehrlich, G.R. Matsueda, M.N. Margolies, E. Haber

引用次数: 4

Interactions of radiolabeled tuftsin with human neutrophils 放射性标记簇状细胞与人中性粒细胞的相互作用

Immunochemistry Pub Date : 1978-12-01 DOI: 10.1016/0161-5890(78)90125-6

Raghavan M.G. Nair , Bruce Ponce , Hugh H. Fudenberg

{"title":"Interactions of radiolabeled tuftsin with human neutrophils","authors":"Raghavan M.G. Nair , Bruce Ponce , Hugh H. Fudenberg","doi":"10.1016/0161-5890(78)90125-6","DOIUrl":"10.1016/0161-5890(78)90125-6","url":null,"abstract":"<div>Tuftsin, the phagocytosis-stimulating peptide, was labeled with [14C] or [125I] at the C-terminal or N-terminal portions of the molecule and the specific interactions of the corresponding radiolabeled tuftsin with human neutrophils, lymphocytes, or monocytes were studiedin vitro. Neutrophils bound 72.2 ± 10.3%, of the14C- or125I-labeled tuftsin in the incubation medium. When the label was incorporated at the N-terminal portion, the binding was reduced to 10%, indicating that the N-terminus is essential for the activity. Lymphocytes and monocytes also showed specific binding sites for labeled tuftsin, but the percentage binding was lower. The differences were not significant. Addition of varying amounts of unlabeled tuftsin to the labeled tuftsin-neutrophil complex, indicated quantitative competition for the binding sites on the cells. Preincubation of the neutrophils with chicken antituftsin abolished the binding.These studies indicate that neutrophils, lymphocytes and monocytes possess receptor sites for the phagocytosis-stimulating peptide. The enzymatic cleavage and generation of tuftsin from leukokinin by the action of leukokininase on neutrophils has been suggested to be a major event in phagocytosis. The receptor sites on neutrophils for the tetrapeptide tuftsin, evidenced by our present work, provide a valuable link towards the elucidation of the mechanism of phagocytosis-stimulation. The presence of similar binding sites for tuftsin on lymphocytes and monocytes indicates a probable role for these cell populations as well, in the sequence of events during phagocytosis. Splenectomized or asplenic patients who have frequent infections may be having defective Fc receptors on these cells or these patients may be deficient in the particular subclass of IgG and/or the specific enzyme which cleaves tuftsin from it.</div>","PeriodicalId":13265,"journal":{"name":"Immunochemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1978-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0161-5890(78)90125-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11785115","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}

引用次数: 42

Immunogenicity of glutaraldehyde treated homologous monomeric albumin in rabbits 戊二醛处理兔同源单体白蛋白的免疫原性

Immunochemistry Pub Date : 1978-12-01 DOI: 10.1016/0161-5890(78)90128-1

Doina Onica, Maria-ana Dobre, Rodica Lenkei

{"title":"Immunogenicity of glutaraldehyde treated homologous monomeric albumin in rabbits","authors":"Doina Onica, Maria-ana Dobre, Rodica Lenkei","doi":"10.1016/0161-5890(78)90128-1","DOIUrl":"10.1016/0161-5890(78)90128-1","url":null,"abstract":"<div>Previous studies (Onicaˇ et al., 1978) have shown that glutaraldehyde polymerized homologous albumin is immunogenic in rabbits. The reaction mixture consisted of high proportion of polymeric and oligomeric molecules, but a small quantity of monomeric ones. The present investigation shows that the monomeric fraction isolated from the reaction mixture is altered in comparison with untreated monomeric albumin. The modification produced in the homologous monomeric albumin by glutaraldehyde conferred to the molecule immunogenic properties, due to the presence of new antigenic sites (haptenic determinants). Glutaraldehyde treatment induced similar haptenic determinants on albumins of different origins as shown by the cross-reactivity between glutaraldehyde treated human and rabbit albumin, which precipitate both with human and rabbit antibodies. Rabbit antibodies were shown to be specific both for the glutaraldehyde modified monomeric albumin and the “aged” fraction which exist in albumin stored either in dry state (commercial albumin) or in solution at 37°C. The same antibodies failed to react with freshly prepared albumin. Our data strongly suggest that the glutaraldehyde treatment alter the monomeric albumin in a similar way asin vitro “ageing” does.</div>","PeriodicalId":13265,"journal":{"name":"Immunochemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1978-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0161-5890(78)90128-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11307154","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}

引用次数: 21

Immunoglobulin biosynthesis in mouse thymus cells. The expression of α and μ chains in BALB/c, C57BL and intercrossed hybrid mice 小鼠胸腺细胞免疫球蛋白的生物合成。α链和μ链在BALB/c、C57BL和杂交小鼠中的表达

Immunochemistry Pub Date : 1978-12-01 DOI: 10.1016/0161-5890(78)90122-0

Nitza Lahat , Chaya Moroz, Israel Ashkenazi

引用次数: 4

Production and study of antibody produced aganist rat cadmium thionein 大鼠镉硫蛋白抗体的制备与研究

Immunochemistry Pub Date : 1978-12-01 DOI: 10.1016/0161-5890(78)90119-0

Ronald J. Vander Mallie, Justine S. Garvey

引用次数: 81

Formation of non-covalently linked IgM polymers: Dependence on the protein sulfhydryl groups and zinc ions 非共价连接IgM聚合物的形成:对蛋白质巯基和锌离子的依赖

Immunochemistry Pub Date : 1978-12-01 DOI: 10.1016/0161-5890(78)90124-4

Trond Eskeland

{"title":"Formation of non-covalently linked IgM polymers: Dependence on the protein sulfhydryl groups and zinc ions","authors":"Trond Eskeland","doi":"10.1016/0161-5890(78)90124-4","DOIUrl":"10.1016/0161-5890(78)90124-4","url":null,"abstract":"<div>Splitting of native polymeric IgM to tree non-covalently linked half sub-units and free J-chains was obtained by reduction with 0.2M mercaptoethanol. Removal of the reducing agent by dialysis for 24 hr or several days in the presence of 10 mm of cheluting agents gave no polymers, while dialysis in the presence of 20 μM zinc ions gave up to 97% of polymers. The polymers showed a sedimentation rate and protein profile in the ultracentrifugc and J-chain content similar to that of native IgM.The polymers made by dialysis for 24 hr were non-covalently linked since they were split by iodoacetamide orN-ethyl maleimide to free non-covalently linked half sub-units and free J-chains and by sodium dodecyl sulphate mostly to free chains. Of the polymeric molecules prepared by dialysis for several days, some of the molecules were found to be stabilized by disulphide bridges.It was concluded that in order to obtain IgM polymersin vitro from reduced IgM, the sub-units and J-chains must have their sulfhydryl groups intact and zinc ions must be present. It seems likely that the formation of covalently linked IgM polymers alsoin vivo is preceded by the formation of non-covalently linked polymers.</div>","PeriodicalId":13265,"journal":{"name":"Immunochemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1978-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0161-5890(78)90124-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11327885","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}

引用次数: 3

Characterization of affinity-labeled fluorescyl ligand to specifically-purified rabbit IgG antibodies 特异性纯化兔IgG抗体亲和标记荧光配体的鉴定

Immunochemistry Pub Date : 1978-12-01 DOI: 10.1016/0161-5890(78)90121-9

Robert M. Watt, Edward W. Voss Jr.

{"title":"Characterization of affinity-labeled fluorescyl ligand to specifically-purified rabbit IgG antibodies","authors":"Robert M. Watt, Edward W. Voss Jr.","doi":"10.1016/0161-5890(78)90121-9","DOIUrl":"10.1016/0161-5890(78)90121-9","url":null,"abstract":"<div>Fluorescein isothiocyanate was reacted with purified rabbit anti-fluorescyl IgG antibodies under defined conditions. Relative to the normal IgG control, significantly more ligand was conjugated to the purified antibody which was then inhibited from further binding with radioactively labeled ligand (3H-N-acetylfluorescein amine). Fluorescyl ligand conjugated to purified antibody preparations exhibited a red spectral shift characteristic of specifically bound fluorophore. Fluorescence of ligand conjugated to antibody was quenched about 95% relative to ~ 90% for ligand reversibly bound. The quantum yield (Φ) of the former is indicative of a thiocarbamyl linkage within the antibody-active site. Fluorescence lifetime (t) measurements by phase and modulation showed a close correlation between liganded and affinity-labeled antibody relative to free ligand and fluorescyl conjugated non-antibody proteins. The fluorescyl-affinity label was not dissociated from the antibody-active site upon denaturation of the protein in 6M guanidine-HCl. Reduction, alkylation and resolution of H and L chains in two different dispersing agents showed that the ligand remained attached to either chain. Fluorescyl ligand bound to high affinity IgG (i.e. non-affinity labeled) was quantitatively released under conditions required for H and L chain production. The fluorescence of affinity labeled ligand was enhanced in high concentrations of deuterium oxide. The latter is characteristic of ligand bound specifically to the antibody active site and is not observed with fluorescein covalently conjugated to non-specific Ig.</div>","PeriodicalId":13265,"journal":{"name":"Immunochemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1978-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0161-5890(78)90121-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11950651","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}

引用次数: 39