Neuraminidase-augmented anticarcinoembryonic antigen (CEA)-complement lysis of human colon tumor cells: lack of correlation with anti-CEA-mediated K-cell lysis and iodine-125 binding.
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Biomedical subjects
Publications and source records attributed to J D Schmale.
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Fluorescein-labeled anti-human globulins were examined to determine the need for standardization of conjugates used in the fluorescent treponemal antibody-absorption (FTA-ABS) test. Twenty-one of 33 conjugates submitted by commercial manufacturers to the Reagents Control Activity, Venereal Disease Research Laboratory, for evaluation in the FTA-ABS test were available for study. Conjugates, after evaluation in FTA-ABS performance tests, were examined by immunoelectrophoresis, by titration against immunoglobulins G and M (IgG, IgM) with FTA-ABS techniques, and by the biuret protein and fluorescein diacetate methods for determining fluorescein to protein (F/P) ratios. The conjugates were predominately anti-IgG globulin with anti-light-chain activity. Differences were noted in the ability of some conjugates to detect IgM antibody. The F/P ratios of those conjugates that could be determined varied from 2.6 to 17.8 mug of fluorescein per mg of protein. The need to identify and standardize both the immunologic capabilities and the optimum F/P ratio for FTA-ABS test conjugates is presented.
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Treponema pallidum can only be cultured in living animal tissue, such as rabbit testes. However, the extract of these organisms from the testicular material leaves the T. pallidum contaminated with tissue debris. This paper describes the separation of T. pallidum from the debris by continuous-particle electrophoresis. The importance of equilibration time before electrophoresis is discussed.
An antigen isolated from Neisseria gonorrhoeae protoplasm reacted well in a flocculation procedure with sera from 86% of the females and 68% of the males infected with gonorrhea; the reactions with sera from presumed noninfected individuals were approximately 12%.
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Two antigen preparations, the soluble antigen and a fraction 1 thereof, isolated in the course of a systematic study of the various antigens of the virulent gonococcus, have been investigated for their ability to serve as antigens for the detection of antibody in patients infected with the gonococcus. The soluble antigen was reactive with 88.2% of the sera from infected females, and fraction 1 was reactive with 71.6% of the sera. Of sera from infected males, only 27.6% reacted with the soluble antigen and only 20.4% with fraction 1. Of sera from individuals presumed free of gonococcal infection, approximately 4% reacted with the soluble antigen; none reacted with fraction 1. This study suggests that these antigens might be adaptable to the detection of human gonococcal antibody, especially in the female.
With the use of the agar-gel-diffusion and complement-fixation techniques, it was shown that protoplasm from different gonococcal isolates reacted with sera from some humans with a history of gonorrhea but did not react with "normal" human sera. The reactive antigen(s) could be partially separated from the other antigens by passing the gonococcal protoplasm through Sephadex G-200. The antigen(s) reacting in the gel-diffusion and complement-fixation tests appeared in the same fraction. On the basis of Sephadex gel filtration, the molecular weight of this antigen(s) is probably greater than 200,000.
Ion-exchange chromatography was used to isolate a fraction from disrupted gonococci which reacts with sera from patients with gonococcal disease in complement-fixation and gel-diffusion tests. This antigenic fraction was shown to be the same as that previously described as having been isolated by gel filtration. The method reported here has the advantage of greater rapidity of isolation together with some improvement in purity.