{"title":"The binding of protein A of immunoglobulin G and of Fab and Fc fragments.","authors":"C Endresen","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Results are presented to show that protein A (pA) may fix to the Fab region of IgG outside the antigen binding site. Thus, pA-reactive Fab fragments were isolated both from specific anti-egg albumin and specific anti-measles virus antibodies. A probable significance of this Fab reactivity in the precipitation reaction between IgG and pA is discussed. Reactive IgG from human, guinea pig, rabbit, and porcine normal sera all showed similar avidity towards pA. Slight differences between IgG subclasses were, however, observed. The avidity of pA-reactive Fab and Fc fragments, isolated from normal porcine IgG, was highest in the latter.</p>","PeriodicalId":75411,"journal":{"name":"Acta pathologica et microbiologica Scandinavica. Section C, Immunology","volume":"87C 3","pages":"185-9"},"PeriodicalIF":0.0,"publicationDate":"1979-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11689438","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":"Cytological events in allo-stimulated lymphocytes triggered by exposure to stimulatory alloantigens. II. Changes in the areal density of cytoplasmic vacuoles and in the subcellular localization of acid phosphatase.","authors":"P B Poulsen, L H Nielsen","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>H-2b lymphocytes were sensitized against H-2d alloantigens by lymphocyte culture reaction and incubated with H-2d mastocytoma cells. The interaction between lymphoid cells and mastocytoma cells was stopped by fixation with glutaraldehyde. The areal density of the cytoplasmic vacuoles as well as the subcellular localization of acid phosphatase in lymphocytes were examined by electron microscopy. Two populations of lymphocytes were observed, small lymphocytes with heterochromatic nuclei and larger lymphocytes (lymphoblasts) with euchromatic nuclei. Only the lymphoblasts showed change following interaction with target cells. The vacuole area in percent of cytoplasmic area (vacuole areal density) of sensitized lymphoblasts increased during the first 30 minutes and from the third to fourth hour of interaction with target cells. Acid phosphatase staining was observed in the Golgi apparatus of the lymphoblasts after 30 minutes of interaction. Multivesicular bodies showed acid phosphatase staining within 20 minutes of interaction with target cells. After 20 minutes of interaction, phagosomes containing myelin figures were formed. These phagosomes also showed acid phosphatase staining and during the next hours of interaction their number increased over the number of multivesicular bodies.</p>","PeriodicalId":75411,"journal":{"name":"Acta pathologica et microbiologica Scandinavica. Section C, Immunology","volume":"87C 3","pages":"203-11"},"PeriodicalIF":0.0,"publicationDate":"1979-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11376386","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":"Activation of human monocytes by mediators from lymphocytes stimulated with Corynebacterium parvum.","authors":"J Hammerström, G Unsgaard, J Lamvik","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Human monocytes activated in vitro by lymphokine-containing supernatants of autologous or allogeneic lymphocytes stimulated in vitro by Corynebacterium parvum (CP) expressed increased ability to suppress DNA-synthesis in a human tumour cell line. Monocyte activation was not dependent on in vitro differentiation of monocytes, enhanced cytostatic ability being observed at all stages of in vitro differentiation. The lymphokine-induced cytostatic ability was not affected by intensive washing and trypsin treatment of the activated monocytes, but disappeared during 48 hours of in vitro culture of the activated cells. The increased cytostatic ability of lymphokine-activated monocytes did not seem to be due to stable supernatant factors released from monocytes. CP stimulated DNA-synthesis in peripheral blood lymphocytes of 28 normal donors, thus confirming the mitogenic effect of CP on human lymphocytes. Lymphokine production in response to CP correlated with the magnitude of DNA-synthesis, but appeared before DNA-synthesis could be detected in the lymphocytes.</p>","PeriodicalId":75411,"journal":{"name":"Acta pathologica et microbiologica Scandinavica. Section C, Immunology","volume":"87C 3","pages":"167-75"},"PeriodicalIF":0.0,"publicationDate":"1979-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11689437","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":"Examination of parotid saliva for antibodies reacting with Streptococcus mutans, lipoteichoic acid and peptidoglycan by the enzyme-linked immunosorbent assay.","authors":"D Bratthall, A Carlén, K W Knox, A J Wicken","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Human parotid saliva was investigated for the presence of IgA antibodies reacting with Streptococcus mutans, lipotechoic acid (LTA) and peptidoglycan. By using an enzyme-linked immunosorbent assay, ELISA, it was shown that the salivas of 12 subjects contained antibodies reacting with S. mutans serotype c and d and with LTA. Six salivas were tested against peptidoglycan but these tests indicated only low levels of antibodies. Absorption of saliva with whole cells of S. mutans inhibited the homologous reaction by up to 87% and the reaction with LTA by up to 52%. Also prior treatment of saliva with LTA caused a decrease in the salivary IgA reaction with LTA and with whole cells of S. mutans. Addition of peptidoglycan to saliva did not markedly affect the salivary IgA reaction with S. mutans. The data show that LTA may be responsible for part of the salivary IgA reaction with whole cells of S. mutans. The significance of LTA in this reaction may vary between different subjects and for different serotypes of S. mutans.</p>","PeriodicalId":75411,"journal":{"name":"Acta pathologica et microbiologica Scandinavica. Section C, Immunology","volume":"87C 3","pages":"251-5"},"PeriodicalIF":0.0,"publicationDate":"1979-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11309873","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 human mixed lymphocyte reaction responder and stimulator capacities of highly purified T- and non-T cells and the role of monocytes.","authors":"P Hokland, I Heron","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>E-rosette sedimentation with AET treated sheep red blood cells and human lymphocytes provieded a source of highly purified T- and non-T cells. Together with unseparated cells these were tested for responder and stimulator capacities in the mixed lymphocyte reaction, and it was found that the non-T cells were weak, but consistent responders only when T cells were present as stimulators. On the other hand, T-T combinations always exhibited weak proliferation demonstrating that T cells possess stimulator capacities. Adherent cells grown on Petri dishes were found to exert a dual function: as helper cells in low, and suppressor cells in high concentrations.</p>","PeriodicalId":75411,"journal":{"name":"Acta pathologica et microbiologica Scandinavica. Section C, Immunology","volume":"87C 3","pages":"191-6"},"PeriodicalIF":0.0,"publicationDate":"1979-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11376385","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":"Lymphocytes from adenoid vegetations: proliferative responses in vitro as compared to blood lymphocytes.","authors":"H H Mogensen, K I Meistrup-Larsen, V Andersen","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Thymidine incorporation by lymphocytes obtained from adenoids (AVL) and blood (PBL) were compared in 27 children undergoing adenoidectomy. Optimal conditions as regards cell number and duration of culture were worked out. The spontaneous thymidine incorporation was higher in PBL than in AVL. In cultures stimulated by polyclonal activators or by PPD, the responses of PBL were higher. The dose-response curves for PBL and AVL after stimulation with killed H. influenzae were different: PBL showed a higher response, the optimal antigen concentration was lower for PBL, and the responsiveness to suboptimal antigen concentrations wash higher in PBL than in AVL.</p>","PeriodicalId":75411,"journal":{"name":"Acta pathologica et microbiologica Scandinavica. Section C, Immunology","volume":"87C 3","pages":"197-202"},"PeriodicalIF":0.0,"publicationDate":"1979-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11528115","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}
P Christensen, A Grubb, R Grubb, G Samuelsson, C Schalén, M L Svensson
{"title":"Demonstration of the non-identity between the Fc receptor for human IgG from group A streptococci type 15 and M protein, peptidoglycan and the group specific carbohydrate.","authors":"P Christensen, A Grubb, R Grubb, G Samuelsson, C Schalén, M L Svensson","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>After electrophoresis of an alkaline extract of type 15 group A streptococci, three main precipitation lines were obtained in diffusion experiments against commercial human polyclonal IgG (lines 1, 2 and 3). Nineteen of 23 sera (83%) from apparently healthy human individuals gave line 3, while 6 of them (26%) gave line 1. The sera giving line 1 did also give line 3. Line 2 was obtained with 2 sera only, also giving lines 1 and 3. Line 3 was caused by a streptococcal Fc-receptor for human IgG, since the line could be displaced by addition of Fc-fragments, but not Fab-fragments of pooled human IgG. Line 1 was shown to be different from line 3, since (1) line 1 was suppressed in contrast to line 3 on absorption of a human serum or commercial polyclonal human IgG with S. aureus; and (2), line 1 was suppressed by Fab-fragments but not Fc-fragments of polyclonal human IgG. Line 2 could be inhibited by addition of peptidoglycan to commercial polyclonal human IgG or a human serum investigated. Another line, 4, obtained in diffusion experiments involving electrophoretically separated alkaline extract of type 15 group A streptococci was type-specific as shown by rabbit antisera to streptococci type M1, M8, M15, and T44, and disappeared on trypsinization of the extract. The component responsible for line 4 in the streptococcal extract, judged to be type-specific M protein, had a mobility different from the component responsible for line 3 in electrophoresis.</p>","PeriodicalId":75411,"journal":{"name":"Acta pathologica et microbiologica Scandinavica. Section C, Immunology","volume":"87C 3","pages":"257-61"},"PeriodicalIF":0.0,"publicationDate":"1979-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11591309","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":"Fractionation of connective-tissue-activating factors from the culture medium of silica-treated macrophages.","authors":"M Aalto, E Kulonen","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The medium of cultured, SiO2-treated peritoneal macrophages contained a factor which enhances the incorporation of labelled proline to collagen and other proteins in granulation tissue slices, cells and polysomes. Simultaneously, the activity of alkaline RNase in the whole medium was decreased in comparison with the corresponding control. Polyvinylpyridine-N-oxide, PVNO, protected the macrophages against SiO2. Latex-particles and E. coli lipopolysaccharide decreased the RNase activity in the macrophage medium, but unlike SiO2 did not cause liberation of the collagen synthesis-stimulating factor. Fractionation of the medium by gel filtration chromatography showed the SiO2-pretreatment to have caused a very significant decrease in the aggregation state of RNase. The fraction from gel filtration chromatography that contained the SiO2-liberated factor stimulating collagen synthesis also contained the disaggregated RNase. There was no RNase-activity in the control sample. A homogenous protein (mol. wt. 14,300) was isolated with repeated gel filtrations from the medium of silica-treated macrophages. It increased the incorporation of 3H proline and 3H thymidine into cultured granuloma cells.</p>","PeriodicalId":75411,"journal":{"name":"Acta pathologica et microbiologica Scandinavica. Section C, Immunology","volume":"87C 3","pages":"241-50"},"PeriodicalIF":0.0,"publicationDate":"1979-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11440156","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":"Isolation of enzymatically derived fragments of porcine IgG and an examination of their reactivity against staphylococcal protein A.","authors":"C Endresen","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Papain digestion of porcine IgG in the absence of cysteine resulted in a rather poor yield of fragments (less than 5 per cent). In the presence of cysteine, 70 to 80 per cent of the IgG was degradated in 4 h. Fragments with molecular weight of about 100,000 and 50,000 were separated by gel filtration. The minor fraction (mol. wt. 100,000) most probably consisted of F(c)2 fragments. Fab/c fragments with both Fc and Fab determinants, and also probably some F(ab)2-like fragments. The F(c)2 fragments appeared to be a dimer of Fc stabilized by disulphide bonds. The second main fraction (mol. wt. 50,000) contained Fc and Fab fragments. Mild reduction of the Fc fragments resulted in Fc subfragments of different sizes, thus indicating that papain cleavages had occurred on different spots in the Fc chain. Non-reduced Fc fragments therefore seem to consist of several Fc subfragments stabilized by disulphide bonds. The protein A reactivity of the isolated Fc fragments were rather low compared to the reactivity of intact IgG, respectively 5--15 and 90 per cent. In addition, protein A reactive Fab fragments were isolated from normal porcine IgG.</p>","PeriodicalId":75411,"journal":{"name":"Acta pathologica et microbiologica Scandinavica. Section C, Immunology","volume":"87C 3","pages":"177-83"},"PeriodicalIF":0.0,"publicationDate":"1979-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11333730","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":"Electron microscopy of treponemes subjected to the Treponema pallidum immobilization (TPI) test. I. Comparison of immunoimmobilized cells and control cells.","authors":"K Hovind-Hougen, H A Nielsen, A Birch-Andersen","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The ultrastructure of cells of T. pallidum Nichols subjected to the TPI test was studied in negatively stained specimens. Cells incubated in basal medium to which was added either human syphilis serum or heated guineapig serum (GPS) showed a normal morphology. This was also the cause for cells incubated with basal medium to which was added either human syphilis serum and heated GPS or normal human serum and unheated GPS. By dark-field microscopy cells obtained from these different incubation mixtures were found to be motile. In contrast, cells incubated in basal medium to which was added human syphilis serum and unheated GPS were all immobilized, and in the electron microscope they presented a morphology strikingly different from that of normal cells. The immunoimmobilized cells were swollen and their surface was completely covered with a layer of fuzzy material. The nature of this material and its possible role in rendering the treponemes immobile is discussed.</p>","PeriodicalId":75411,"journal":{"name":"Acta pathologica et microbiologica Scandinavica. Section C, Immunology","volume":"87C 3","pages":"217-22"},"PeriodicalIF":0.0,"publicationDate":"1979-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11591308","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}