{"title":"Simple method of circulating immune complex detection in human sera by polyethylene glycol precipitation.","authors":"V Hasková, J Kaslík, I Ríha, I Matl, J Rovenský","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A rapid test for detection of circulating immune complexes in a small serum sample was developed to facilitate clinical diagnosis of immune complex disorders. The test is based on a selective precipitation of soluble circulating complexes of antigen-antibody in 3.75% concentration of high-molecular polyethylene glycol. Precipitation is followed photometrically at 450 nm, 1 cm cuv. after 1 h incubation at room temperature. Comparison of E450 values in groups of patients with immune complex disorders, such as rheumatoid arthritis, systemic lupus erythematosus and glomerulonephritis, with healthy controls or patients with non-immunological disorders revealed highly significant differences. Sera of all patients with high clinical activity of disease exhibited positive reaction. In 121 human sera the results of this examination were compared with the results of C 1 q binding test. There was 73.5% agreement between the results of both methods. Our test is more rapid, suited for routine clinical use.</p>","PeriodicalId":23935,"journal":{"name":"Zeitschrift fur Immunitatsforschung. Immunobiology","volume":"154 4","pages":"399-406"},"PeriodicalIF":0.0,"publicationDate":"1978-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11877601","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":"Studies on the immune response in chickens II. Functions of carrier-reactive cells in anti-hapten responses.","authors":"F Nagase, I Nakashima, N Kato, K Yagi","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":23935,"journal":{"name":"Zeitschrift fur Immunitatsforschung. Immunobiology","volume":"154 3","pages":"268-83"},"PeriodicalIF":0.0,"publicationDate":"1978-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11300547","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":"Effect of human immunoglobulin preparations on Fc rosette formation between anti-D-coated erythrocytes and lymphocytes.","authors":"H Ishiyama, K Okuyama, K Masuda, J Yasuda","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Human immunoglobulin (Ig) preparations were tested for their inhibitory effect on Fc rosette formation between anti-D-coated human erythrocytes and lymphocytes, as compared to their complement activating capacity. Both of the two biological activities ascribed to the sites in the Fc portion of the IgG molecules were found to be reduced in the pepsin-treated, as well as in the S-sulfonated Ig preparations, as compared to the activities of the normal human Ig preparation. In the plasmin-treated Ig preparation, which was found to be composed of three major components: plasmin-Fab, plasmin-Fc and plasmin-resistant IgG, the activity of inhibiting the Fc rosette formation was well retained, in contrast to its low complement activating capacity.</p>","PeriodicalId":23935,"journal":{"name":"Zeitschrift fur Immunitatsforschung. Immunobiology","volume":"154 4","pages":"387-98"},"PeriodicalIF":0.0,"publicationDate":"1978-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11369060","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":"Characteristics of soluble T-cell derived factors(s) which can induce non-immune murine macrophages to exert anti-Toxoplasma activity.","authors":"K K Sethi, H Brandis","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":23935,"journal":{"name":"Zeitschrift fur Immunitatsforschung. Immunobiology","volume":"154 3","pages":"226-42"},"PeriodicalIF":0.0,"publicationDate":"1978-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11521391","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":"Type-specific and non-type-specific reactions of purified M protein preparations.","authors":"O Kühnemund, J Havlicek, W Köhler","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>M proteins of type 1 and type 12 Streptococcus pyogenes were extracted by means of phage-associated lysin and purified by ion-exchange chromatography on CM and DEAE cellulose. Molecular weight distributions were studied by gel chromatography on Biogel A 0.5 m in a 6 molar urea solution and by SDS electrophresis. Serological activities were studied by the complement-fixation reaction and immunodiffusion and were compared with the estimated molecular weights. Type-specific and non-specific activity was found to be located on the same polypeptide chain of a size of 2 X 10(4) daltons (type 1) and 1.5 X 10(4) daltons (type 12). These serologically active chains are in preparations purified by chromatographic methods accompanied by polypeptides of different sizes which are held together by noncovalent bonds thus forming molecules above 4 X 10(4) daltons.</p>","PeriodicalId":23935,"journal":{"name":"Zeitschrift fur Immunitatsforschung. Immunobiology","volume":"154 3","pages":"197-207"},"PeriodicalIF":0.0,"publicationDate":"1978-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11316930","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}
J Goudswaard, A Noordzij, R H van Dam, J A van der Donk
{"title":"Quantification of turkey immunoglobulins IgA, IgM and IgG in serum and secretions.","authors":"J Goudswaard, A Noordzij, R H van Dam, J A van der Donk","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The immunoglobulins IgA, IgM and IgG of the turkey were quantitated in individual serum samples as well as in pooled sera. The variability of Ig levels in normal, healthy birds was quite high: IgA: mean value 0.633 mg/ml (4.0 -x - 2.5 -x); IgM: mean value 4.37 mg/ml (0.5 -x - 1.4 -x) and IgG: mean value 8.92 mg/ml (0.6 -x - 1.7 -x). Immunoglobulin levels in egg-yolk, egg-white, bile and some intraocular tissues were quantitated as well. An interesting finding was, that the forementioned variability was by far not so high with respect to IgG levels in 20 egg-yolk samples: mean value 5.1 mg/ml (0.86 x- - 1.17 -x). Though IgG and IgM could be detected in pooled turkey bile, IgA predominated in this secretion. In aqueous humor, iris tissue and vitreous body only IgG could be detected.</p>","PeriodicalId":23935,"journal":{"name":"Zeitschrift fur Immunitatsforschung. Immunobiology","volume":"154 3","pages":"248-55"},"PeriodicalIF":0.0,"publicationDate":"1978-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11770613","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":"Surface carbohydrate composition of murine thymocytes and of lymph node cells from normal and athymic (nude) mice.","authors":"W Droege, P P Singh, O Lüderitz","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Surface glycoproteins (papain digests) have been isolated from lymph node cells of normal mice which contain mainly T cells, and from lymph node cells of nude (athymic) mice, which essentially represent B cells. Gaschromatographic analysis revealed that the glycoproteins from the lymph node cells of the euthymic mice contain less galactose than the glycoproteins from lymph node cells of the athymic mice, but contain still more galactose than glycoproteins from thymocytes. Lymph node cells from both sources contain about equal amounts of neuraminic acid, while thymocytes contain slightly less sialic acid. The observed differences provide a molecular explanation for the different reactivity of murine B cells and T cells towards soybean agglutinine and other galactose-binding plant lectins.</p>","PeriodicalId":23935,"journal":{"name":"Zeitschrift fur Immunitatsforschung. Immunobiology","volume":"154 3","pages":"243-7"},"PeriodicalIF":0.0,"publicationDate":"1978-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11521392","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":"Genetics of the idiotype of strain AKR antibodies to group A streptococcal carbohydrate; further evidence for a low degree of homology in the VH chromosomal region.","authors":"P Krammer, B A Taylor, K Eichmann","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A new VH gene is described which governs the expression of idiotypes associated with the antibody response of strain AKR mice to Group A streptococcal carbohydrate (A-CHO). This VH gene, termed ACHd, is identified using guinea pig antisera to a pool of strain AKR antibodies to A-CHO. The genetic polymorphism is revealed by quantitative differences in idiotype expression between different inbred strains. In recombinant inbred strains linkage to the Ig-1d allotype allele of strain AKR is demonstrated. In a putative recombinant strain it appears that ACHd maps at a locus different from that of A5A+, another VH gene controlling idiotypes of anti-A-CHO antibodies. This represents a further example of pseudoallelism between related VH genes and lack of homology in the VH chromosomal region. Expression of the ACHd gene was independent of the Ly-2, 3 locus which is associated with kappa chain variants.</p>","PeriodicalId":23935,"journal":{"name":"Zeitschrift fur Immunitatsforschung. Immunobiology","volume":"154 3","pages":"284-95"},"PeriodicalIF":0.0,"publicationDate":"1978-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11316932","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":"Studies on the immune response in chickens I. Effect of various immunization procedures on the primary and secondary antibody responses to bovine serum albumin.","authors":"F Nagase, I Nakashima, N Kato, K Yagi","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Antibody response and generation of immunological memory in chickens after stimulation by bovine serum albumin (BSA) were investigated. A single intravenous injection of BSA induced a relatively high primary antibody response but failed to generate definite memory for the secondary antibody response. Variation in antigen dosage and the time interval between antigen injections did not affect significantly the levels of the primary and secondary antibody responses. The immunogenicity of deaggregated BSA in chickens was as potent as that of aggregated BSA. Soluble adjuvants such as the capsular polysaccharide of Klebsiella pneumoniae, cell wall lipopolysaccharide of Salmonella enteritidis and cell wall peptidoglycan of Staphylococcus epidermidis exhibited little enhancing effect on antibody response and memory. However, stimulation of chickens by BSA emulsified in Freund's adjuvant enhanced generation of memory. Repeated injection of BSA alone also showed a similar effect. It seems likely therefore that in chickens continous antigenic stimulation is required for generation of definite memory. From the present results it has been concluded that the characteristics of the immune response of chickens to BSA resemble those of mammals to T-independent antigens.</p>","PeriodicalId":23935,"journal":{"name":"Zeitschrift fur Immunitatsforschung. Immunobiology","volume":"154 3","pages":"256-67"},"PeriodicalIF":0.0,"publicationDate":"1978-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11877600","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}