Antibody-like Activity to the 2,4-Dinitrophenyl Group in Normal Human Sera

Nature ◽  
1969 ◽  
Vol 221 (5184) ◽  
pp. 960-962 ◽  
Author(s):  
MICHAEL W. BRANDRISS
Keyword(s):  
1966 ◽  
Vol 53 (4) ◽  
pp. 673-680 ◽  
Author(s):  
Torsten Deckert ◽  
Kai R. Jorgensen

ABSTRACT The purpose of this study was to investigate whether a difference could be demonstrated between crystalline insulin extracted from normal human pancreas, and crystalline insulin extracted from bovine and porcine pancreas. Using Hales & Randle's (1963) immunoassay no immunological differences could be demonstrated between human and pig insulin. On the other hand, a significant difference was found, between pig and ox insulin. An attempt was also made to determine whether an immunological difference could be demonstrated between crystalline pig insulin and crystalline human insulin from non diabetic subjects on the one hand and endogenous, circulating insulin from normal subjects, obese subjects and diabetic subjects on the other. No such difference was found. From these experiments it is concluded that endogenous insulin in normal, obese and diabetic human sera is immunologically identical with human, crystalline insulin from non diabetic subjects and crystalline pig insulin.


2003 ◽  
Vol 71 (7) ◽  
pp. 3875-3884 ◽  
Author(s):  
Christian Theilacker ◽  
Fadie T. Coleman ◽  
Simone Mueschenborn ◽  
Nicolas Llosa ◽  
Martha Grout ◽  
...  

ABSTRACT Deterioration of lung function in patients with cystic fibrosis (CF) is closely associated with chronic pulmonary infection with mucoid Pseudomonas aeruginosa. The mucoid exopolysaccharide (MEP) from P. aeruginosa has been shown to induce opsonic antibodies in mice that are protective against this chronic infection. MEP-specific opsonic antibodies are also commonly found in the sera of older CF patients lacking detectable P. aeruginosa infection. When used in a human vaccine trial, however, MEP only minimally induced opsonic antibodies. To evaluate whether conjugation of MEP to a carrier protein could improve its immunogenicity, we bound thiolated MEP to keyhole limpet hemocyanin (KLH) by using succinimidyl-4-(N-maleimidomethyl)cyclohexane-1-carboxylate (SMCC) as a linker. In contrast to the native MEP polymer, the MEP-KLH conjugate vaccine induced high titers of MEP-specific immunoglobulin G (IgG) in C3H-HeN mice and in a rabbit. Sera from mice immunized with MEP-KLH conjugate, but not from animals immunized with comparable doses of native MEP, demonstrated opsonic killing activity. Vaccination with MEP-KLH conjugate induced opsonic antibodies broadly cross-reactive to heterologous mucoid strains of P. aeruginosa. Preexisting nonopsonic antibodies to MEP are found in normal human sera, including young CF patients, and their presence impedes the induction of opsonic antibodies. Induction of nonopsonic antibodies by either intraperitoneal injection of MEP or injection or feeding of the cross-reactive antigen, seaweed alginate, reduced the level of overall IgG elicited by follow-up immunization with the MEP-KLH conjugate. However, the opsonic activity was lower only in the sera of MEP-KLH conjugate-immunized mice with preexisting antibodies induced by MEP but not with antibodies induced by seaweed alginate. Immunization with MEP-KLH elicited a significant proportion of antibodies specific to epitopes involving O-acetate residues, and this subpopulation of antibodies mediated opsonic killing of mucoid P. aeruginosa in vitro. These results indicate that conjugation of MEP to KLH significantly enhances its immunogenicity and the elicitation of opsonic antibodies in mice and rabbits, that the conjugate induces opsonic antibodies in the presence of preexisting nonopsonic antibodies, and that opsonic antibodies to MEP are directed at epitopes that include acetate residues on the uronic acid polymer.


1975 ◽  
Vol 8 (1-2) ◽  
pp. 17-28 ◽  
Author(s):  
F. Shakib ◽  
D.R. Stanworth ◽  
R. Drew ◽  
D. Catty

1982 ◽  
Vol 28 (2) ◽  
pp. 306-310 ◽  
Author(s):  
E Reiss ◽  
L Stockman ◽  
R J Kuykendall ◽  
S J Smith

Abstract Candida albicans mannan was added to normal human sera and the resulting complexes were dissociated by boiling (boil) with EDTA or by alkali treatment (bead method). The mannan released was detected by "sandwich" enzyme immunoassay (EIA) or by EIA inhibition. Each EIA took 2.3 h to perform. The total time for the boil-EIA combination was 2.7 h and for the bead-EIA, 3.8 h. The temperature favorable for antigen--antibody incubation was 4 degrees C. The sandwich EIAs were preferable to EIA inhibition because absorbance was directly proportional to mannan concentration, within-run variation was decreased, and accuracy was increased. The boil-sandwich EIA had the highest sensitivity in the 12.5 to 200 micrograms/L range.


Blood ◽  
1993 ◽  
Vol 82 (5) ◽  
pp. 1402-1409 ◽  
Author(s):  
SM Richards ◽  
TA Olson ◽  
JM McPherson

Abstract Recent clinical data have shown that enzyme replacement therapy with macrophage-targeted glucocerebrosidase (GCR) can be effective in treating type 1 Gaucher disease. Sera from 262 patients, repeatedly infused with GCR, were assessed for the presence of antibodies to this therapeutic protein. Patient serum samples obtained at 3-month intervals were assessed by enzyme-linked immunosorbent assay and those with values greater than two standard deviations above the mean value obtained with a pool of normal human sera were further characterized by radioimmunoprecipitation. At the time of these analyses, the duration of patient treatment varied from 3 months to approximately 3 years. Of the 262 patients analyzed, 34 (12.9%) showed IgG antibodies, as confirmed by radioimmunoprecipitation. All patients who seroconverted did so within 1 year of treatment. The predominant antibody developed was the IgG1 subclass. Fourteen patients in the study experienced periodic symptoms suggestive of immediate hypersensitivity. Nine of these 14 patients had antibody to GCR as determined by radioimmunoprecipitation, whereas 5 patients were antibody negative. There was no evidence of the development of IgE antibodies in these 14 patients. The presence of GCR antibodies did not appear to effect efficacy of therapy in any of the patients treated to date.


1948 ◽  
Vol 87 (1) ◽  
pp. 57-70 ◽  
Author(s):  
T. N. Harris

Complement-fixing antibodies to the cytoplasmic particles (CP) and to the S fraction of streptococcal nucleoproteins are present in normal human sera, the range of concentrations varying among the age groups. The titer of these antibodies rises between the first half-week and the 3rd week of scarlet fever, in more than 80 per cent of the cases. The titers then remain elevated for at least 4 months. In children, 91 per cent of the normal sera examined showed anti-CP titers up to 32; 87 per cent of sera in active rheumatic disease had titers above this level. Corresponding data with S fell in the same range of percentage distribution. Anti-CP and anti-S titers remained elevated long after the rheumatic process had reached quiescence. No correlation of serologic titer with the degree of clinical activity was found in the case of either antibody.


1961 ◽  
Vol 39 (10) ◽  
pp. 1567-1574 ◽  
Author(s):  
Catherine F. C. MacPherson ◽  
James B. R. Cosgrove

Two immunologically different gamma globulins were revealed in "normal" cerebrospinal fluid (NCSF) and in multiple sclerosis cerebrospinal fluid (MSCSF) by immunoelectrophoretic analyses, which employed rabbit antisera prepared against NCSF and MSCSF. Since only one gamma-globulin arc was formed on immunoelectrophoretic analyses of normal human sera (NHS) with rabbit anti-CSF sera and repeated absorptions of anti-CSF sera with human serum failed to remove antibodies to the minor gamma globulin, it would appear that the minor gamma globulin is peculiar to CSF. The major gamma globulin of CSF was shown to be immunologically identical with the single gamma globulin of serum as judged by the fusion of their respective precipitin arcs. The major and minor gamma globulins of NCSF could not be distinguished from those of MSCSF by any of the rabbit antisera used. However, the ends of the precipitin arc formed by the major gamma globulin of NCSF with its homologous antibody became frayed and sometimes doubled indicating it to be immunologically less homogeneous than the gamma globulin of serum. The two gamma globulins of MSCSF and the minor gamma globulin of NCSF migrated more slowly than the major gamma globulin of NCSF. In comparison with NHS, the immunoelectrophoretic patterns of CSF developed with anti-CSF sera were characterized, in the alpha-2 zone, by a greater number of stronger arcs. Experiments on absorbed anti-CSF sera indicated that this was due to differences in the relative concentrations of the various components of this zone in the two fluids.


1969 ◽  
Vol 67 (1) ◽  
pp. 41-47 ◽  
Author(s):  
J. S. Oxford ◽  
C. W. Potter

SUMMARYThe inactivation kinetics of CELO virus were studied in the presence of 1/4000 formaldehyde. Inactivation of the virus by formaldehyde at 4° C. was not complete after 14 days incubation. Formaldehyde inactivation at 36° C., however, was rapid and no virus was detected after 24 hr. incubation.Neutralizing antibody to CELO virus was detected in 20–88% of sera tested from five flocks of hens. This suggested dissemination of the virus in England and Scotland. However, no CELO virus neutralizing antibody at a serum dilution of 1/8 was detected in 142 normal human sera or in 229 sera from persons who had been immunized with egg grown, inactivated influenza virus vaccine.We would like to thank Professor C. H. Stuart-Harris and Drs J. E. Wilson, D. A. Martin and D. Breeze for their help and their criticisms of the manuscript.Dr G. C. Schild kindly supplied a number of the human sera used in the study. The study was financed in part by the National Fund for Research in Poliomyelitis and other Crippling Diseases and by the British Empire Cancer Campaign.


Blood ◽  
1962 ◽  
Vol 19 (3) ◽  
pp. 379-398 ◽  
Author(s):  
JOHN P. LEDDY ◽  
NORMA C. TRABOLD ◽  
JOHN H. VAUGHAN ◽  
SCOTT N. SWISHER

Abstract Several human pathologic sera containing high titered cold agglutinins were studied to determine whether the serologic activity ascribed to an "incomplete cold antibody" could be separated from the "complete" cold agglutinin activity. Separation was not achieved by physicochemical methods, including zone electrophoresis, density gradient ultracentrifugation, and anion exchange chromatography. Both activities were susceptible to destruction by mercaptans. Neither activity could be differentially absorbed from the sera. Using "Bombay" and I-negative ("i") red cells, a difference in specificity of the two activities for the H or I antigen of human erythrocytes could not be demonstrated. The simplest interpretation of these findings is that there is only one antibody involved, the cold agglutinin, and that the serologic manifestation usually attributed to an additional "incomplete cold antibody", i.e. the production of a positive antiglobulin reaction of the "non-γ-globulin" type, results from an interaction of complement components with the cold agglutinin-erythrocyte complex. Three of these cold agglutinating sera were unreactive with I-negative erythrocytes, in keeping with the reported anti-I specificity of these antibodies. A fourth serum retained moderate, though greatly reduced, activity against these cells, and the interpretation of this finding is discussed. The anti-H specificity of the incomplete cold antibodies in normal human sera was confirmed by their failure to sensitize "Bombay" erythrocytes. This was in sharp contrast to the excellent reactivity of the pathologic sera with these cells, demonstrating that pathologic cold agglutinins are unrelated to the incomplete cold antibodies present in most normal sera.


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