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At least 253 records · Page 14Linked to original sources
PubMed1994

Comparison of indirect haemagglutination test, gel-diffusion precipitin test, and enzyme-linked immunosorbent assay for detection of serum antibodies to Pasteurella multocida in naturally and experimentally infected rabbits.

Enzyme-linked immunosorbent assay (ELISA), gel-diffusion precipitin test (GDPT), and indirect haemagglutination test (IHAT) were evaluated for the detection of antibodies to Pasteurella multocida in both naturally and experimentally infected rabbits. A total of 285 rabbit serum samples from 7 rabbit colonies were tested by ELISA, GDPT, and IHAT, and nasal cultures were taken coincidentally to use as the standard in the serological tests. There was better correlation (98.0%) between the results of ELISA and positive nasal culture than between the GDPT (86.3%) or IHAT (23.5%) and positive nasal culture. In addition, ELISA and GDPT were positive in 26 (11.1%) and 21 (9.0%) of 234 serum samples from nasal culture negative rabbits, respectively. In experimentally infected rabbits, antibodies detected by the ELISA and GDPT began to rise one to 3 weeks post-inoculation. IHAT did not detect antibodies. These results are discussed in terms of value to serodiagnosis of rabbit pasteurellosis.

Animals↗
PubMed1977

A precipitin test for the diagnosis of human abdominal angiostrongyliasis.

A precipitin reaction was observed when sera of cotton rats infected either naturally or experimentally with Angiostrongylus costaricensis were tested by gel double-diffusion against sera obtained from three biopsy-confirmed human cases of A. costaricensis. With immunoelectrophoresis, the antigen was demonstrated in the serum of infected rats. The antibody in the human serum was mostly of the IgG type. No cross reactions were seen with sera from individuals infected with the common intestinal helminths, or individuals serologically positive for Toxocara, A. cantonensis, Chagas' disease, amebiasis, leishmaniasis, toxoplasmosis, or syphilis.

Abdomen↗
PubMed1981

Immunoperoxidase localization by electron microscopy of soluble egg antigen and human IgG in circumoval precipitin reactions around Schistosoma mansoni eggs.

Soluble egg antigen and human IgG were localized by the unlabelled antibody enzyme technique for electron microscopy on Schistosoma mansoni eggs having circumoval precipitin reactions. Reaction products indicating the presence of soluble egg antigen were on portions of the circumoval precipitate outside the egg, between the eggshell and vitelline membrane, and between the vitelline membrane and miracidium inside the egg. Reaction products indicating human IgG were only found on portions of the circumoval precipitate external to the eggshell.

Animals↗
PubMed1988

Quantitative precipitin reaction and enzyme-linked immunosorbent assay of mannans of Candida albicans NIH A-207 and NIH B-792 strains compared.

We assessed the difference between results by enzyme-linked immunosorbent assay (EIA) in plastic support wells and the quantitative precipitin reaction (QPR) in glass test tubes for antigenic mannans and antibodies of two representative Candida albicans strains, NIH A-207 and NIH B-792. We investigated each of four mannan subfractions, with different phosphate contents, for their reactivities to the homologous polyclonal rabbit antiserum. Each series of mannan subfractions showed a reactivity proportional to their phosphate content in EIA, in a similar manner as observed in QPR. Moreover, in EIA, the cross-reactivities between the bulk mannans of the two C. albicans strains and the polyclonal antiserum of a Saccharomyces cerevisiae wild-type strain containing specific antibodies to the non-reducing terminal alpha-1,3-linked D-mannopyranose unit resembled those of the same antigen-antibody reactions in QPR. However, the mannan of C. albicans NIH A-207 strains, a weak antigen in the cross-QPR system, reacted fairly strongly in EIA in its high concentration range, indicating that EIA can be used to detect such an epitope in these mannans in concentrations undetectable by QPR. We conclude that EIA is a useful technique for immunochemical assay of yeast mannans and their antibodies on a smaller scale than with QPR.

Candida albicans↗
PubMed1986

Alpha 1-protease inhibitor in serous effusions: differences in lectin crossed immuno-affinoelectrophoresis precipitin profiles between benign and malignant disease.

Differences in the lectin crossed immuno-affinoelectrophoresis (LCIE) precipitin profile of the antiprotease alpha 1-protease inhibitor (alpha 1-PI) have been detected between serous effusions of benign and malignant origin. Extra proteins with antigenicity towards anti-human alpha 1-PI appear in both malignant pleural effusions and malignant ascitic fluid caused by ovarian cancer that are not detected in effusions of benign origin. These compounds may be protease-antiprotease complexes caused by tumour excretion of proteases into the serous effusions.

Ascitic Fluid↗
PubMed1984

Assay, purification and further characterization of 7S C1q-precipitins (C1q-p) in hypocomplementemic vasculitis urticaria syndrome and systemic lupus erythematosus.

C1q-precipitins (C1q-p) are comprised of 7S IgG with C1q-binding activity found in sera of patients with hypocomplementemic vasculitis urticaria syndrome ( HVUS ) and systemic lupus erythematosis (SLE). We have utilized C1q-coated polystyrene beads to selectively isolate C1q-p and to establish a sensitive and quantitative assay of C1q-p and immune complex activity. Purified C1q-p was comprised of polyclonal IgG which retained 7S sedimentation and solid phase C1q-binding activity at physiological ionic strength both in the presence and absence of normal human sera. No precipitation interaction was observed between C1q-p and fluid-phase C1q or C1 under the conditions tested. Purified C1q-p had no activity in the Raji cell immune complex activity. C1q-p activity also was observed in and purified from SLE serum; this activity was distinguishable from 7S immune complex activity detected by Raji cells which was also present in SLE serum. These studies indicate that C1q-p is a 7S IgG molecule found in HVUS as well as some SLE sera and has activity in C1q-binding but not in Raji cell-binding immune complex assays. These data also suggest that C1q-p is a monomeric, polyclonal IgG with preferential affinity for bound C1q. In addition to its potential role in immune complex disease, C1q-p may also provide an important tool for studying the interaction of immunoglobulin and C1q, and should contribute important information to understanding the pathobiology of immune complex disease.

Antigen-Antibody Complex↗