Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0220723 (PCA)
 4,687 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We tried to prepare hen's egg with low antigenicity for allergy patients. First, we examined the effects of pH, heating temperature and time on antigenicity of egg. Dried whole egg solid (DES) was dissolved in the buffer solution adjusted at various pH and heated at 120 degrees C for 10, 20 and 40 min. As a result the antigenicity didn't significantly decrease. Next, DES was treated with succinic anhydride, sodium hydroxide and was heated. The antigenicity of the resultant modified whole egg solid (MES) was much lower than that of heated whole egg solid. Antigenicity was measured precisely by enzyme immunoassay, inhibition ELISA, RAST inhibition and PCA. It was found that the antigenicity of MES was decreased less than 1/1000 of that of DES. Then SDS-polyacryl-amide gel electrophoresis and gel filtration were performed to clarify the degree of the change of egg proteins. The bands and peaks which corresponded to ovalbumin and ovomucoid known to be major allergenic proteins responsible for egg allergy disappeared and new bands and peaks were detected.
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PMID:[Development of hen's egg with low antigenicity for allergic patients]. 179 64

Allergenicity of three plant abortifacient proteins, trichosanthin (TCS), alpha-momorcharin (alpha-MMC) and beta-momorcharin (beta-MMC) and the kinetics of IgE antibody response against these proteins were studied in C57BL/6N and BALB/cAn mice. These proteins were purified from Chinese medicinal herbs, characterized by biochemical and immunological procedures and found to be homogeneous by PAGE, SDS-PAGE and immunoelectrophoresis. The results obtained were summarized as follows: 1) different levels of IgE antibody responses against TCS, alpha-MMC and beta-MMC were induced when they were injected i.p. as antigen adsorbed onto AI(OH)3 gel into BALB/cAn or C57BL/6N mice on day 0 and day 28; 2) the allergenicity of the proteins was in the order of beta-MMC greater than alpha-MMC greater than TCS; 3) two injections of 10 micrograms or 50 micrograms of TCS or alpha-MMC given at 4 weeks interval without adjuvant elicited a low or undetectable PCA titer, while the same dose given weekly for 5 weeks resulted in high levels of IgE production; and 4) on the basis of PCA observations, no cross immunological reactivity among these three proteins was found, it seemed to support that TCS, alpha-MMC and beta-MMC may be alternately used for inducing abortion.
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PMID:Kinetics of IgE antibody response to trichosanthin alpha-momorcharin and beta-momorcharin in mice. 206 46

Two allergenic components, termed J1 and J2, were isolated from a soluble egg antigen preparation (SEA) of Schistosoma japonicum by anion-exchange chromatography on DE52 and gel chromatography on Sephacryl S-200. The apparent molecular weights of J1 and J2 were 260,000 and 46,000, respectively, by gel chromatography on Sephadex G-150. By SDS-polyacrylamide gel electrophoresis, both J1 and J2 showed apparent homogenicity and their estimated molecular weights were 135,000 and 45,000, respectively. The isoelectric point of J1 (pI 4.9) was similar to that of J2 (pI 4.8). Both J1 and J2 bound to Con A-Sepharose 4B, indicating their glycoprotein nature. The amino acid compositions of J1 and J2 have some similarities. However, phenylalanine and leucine, which contain large hydrophobic groups, were dominant in J1, whereas serine and threonine, which contain a hydroxyl group, were dominant in J2. J1 was sensitive to heating or pronase treatment, whereas J2 was rather stable to these treatments. Both J1 and J2 were sensitive to 0.1 M periodate treatment. When mice were immunized with either J1 or J2 with A1(OH)3 as an adjuvant, anti-J1 or anti-J2 IgE antibody was highly specific to the respective antigens. Since S. japonicum-infected mouse serum has high PCA titer to J1 and J2, these two components are the major allergens of S. japonicum eggs.
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PMID:Isolation of two immunogenically different allergens from Schistosoma japonicum eggs. 303 85

Trypanosoma cruzi chromatin is not condensed in chromosomes during mitosis. In previous studies a characteristic H 1 was not found in SDS or in acid-urea-PAGE. Consequently, it was proposed that the particular behavior of T. cruzi chromatin in dividing cells was due to the absence of an H 1 histone. In the present work, histones from this parasite were systematically characterized by spectrofluorometric analysis, amino acid composition, PAGE in one and in two dimensions, differential extraction with PCA and TCA, immunological cross-reactivity with antisera, and immunoblotting. We conclude that T. cruzi contains all five histones, H 1 presenting solubility and immunological properties similar to those in other species, but with a particular electrophoretic mobility in Triton-PAGE. Thus an explanation other than the absence of H 1 should be offered in order to understand the behavior of T. cruzi chromatin during mitosis. Moreover, histone variants were described by two-dimensional PAGE. The presence of histone variants suggests that they may participate in the regulation of cell proliferation and differentiation of this parasite, as it has been postulated for higher eukaryotes.
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PMID:H 1 histone and histone variants in Trypanosoma cruzi. 312 71

1. Tammar wallaby (Macropus eugenii, Marsupialia) proteins with similar electrophoretic mobilities to calf non-histone chromosomal proteins HMG 1, 2, 14 and 17 are perchloric acid extracted from whole tissues (liver, kidney, spleen, brain and testis) and purified liver nuclei (using PCA or 0.35 M NaCl). 2. Tammar and calf HMG 1 have similar amino acid compositions. 3. Two testis-specific basic proteins co-extracting with HMG-like proteins from both tammar and red kangaroo (Megaleia rufa) are found in whole testis, purified testis nuclei, but not epididymis. 4. Tammar HMG 2 separates into two components on both acid urea and SDS gels. The larger, more basic protein, HMG 2b, is relatively abundant in proliferating tissues (testis, spleen).
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PMID:High mobility group (HMG) proteins in the tammar wallaby Macropus eugenii: quantitative variations between tissues and testis-specific co-extracted proteins. 362 8

By fusion of C3H mouse spleen cells, immunized with a PCA extract from liver metastases of a colon tumor, and Sp2/O-Ag14 myeloma cells, we produced several clones secreting monoclonal antibodies (MAb) with reactivity against carcinoembryonic antigen (CEA). For the screening of the different MAb, an ELISA technique with PCA extract and highly purified CEA coupled with alkaline phosphatase was employed. The specificities of the MAb prescreened with the ELISA technique were analyzed further by immunoprecipitation and separation on SDS-PAGE, followed by enzyme digestion and thin-layer chromatography for fingerprint analysis. The MAb recognized (a) an antigenic determinant present only on CEA, (b) common determinants present on CEA and at least six other molecules separated by SDS-PAGE and (c) antigenic determinants not present on CEA. The fingerprint analysis showed the relationship of the molecules on the basis of protein chemistry.
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PMID:Monoclonal antibodies against CEA. Comparison of the immunoprecipitates by fingerprint analysis. 618 85

A major antigen inducing IgE in mice (DpI) was purified from a crude extract of Dermatophagoides pteronyssinus (D.p.) using Sephacryl S-200 gel filtration, DE52 ion exchange chromatography and isoelectric focusing. This antigen is not one of the major D.p. human allergens. Isoelectric focusing showed a single peak of PCA activity at pI 4.7. Activity followed a broader banding pattern on polyacrylamide gel electrophoresis (PAGE). The molecular weight of DpI estimated from Sephadex G-150 chromatography was 1.7 X 10(5) daltons. Molecular weight calculated from SDS-gels (reducing), however, was 3.7 X 10(4), which may indicate a molecule with a subunit composition. DpI contained no detectable hexose as measured by the phenol-sulfuric acid assay. PCA activity of DpI was stable at 98 degrees C and to treatment with 0.1 M sodium metaperiodate, but destroyed by pronase. DpI represents approximately one per cent of the total protein of crude extracts. Purified DpI displays a specific activity increase of 40 times that of the crude extract with the PCA test. DpI is capable of inhibiting 40% of the binding between crude extract and human IgE, but only at extremely high concentrations. Human IgE was 700 times more sensitive to D.p. crude extract than purified DpI by enzyme immunoassay.
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PMID:Purification of a murine IgE-inducing antigen extracted from the house dust mite, Dermatophagoides pteronyssinus. 704 69

Elevated levels of ovine reaginic antibody were induced by immunization with Ascaris suum antigens. The PCA activity of this antibody persisted in the skin of sheep for 20 days and was abolished by heating to 56 degrees C, suggesting that it was immunoglobulin E. Attempts to isolate IgE from this hyperimmune serum by gel filtration, ion exchange and affinity chromatography resulted in the preparation of a PCA-positive fraction containing proteins with molecular weights of 70, 56 and 22 kD on SDS-PAGE. This preparation was used to raise an antiserum in a rabbit to IgE which was rendered specific by absorption. An antiserum to the heavy chain of ovine IgE was also raised in a rabbit by immunization with a fraction prepared from the 68- to 80-kD region of SDS-PAGE by excision and electroelution. Both antisera were positive in reverse cutaneous anaphylaxis tests and recognized a single protein with a molecular weight of 70-72 kD on SDS-PAGE immunoblotting. The presence of this protein in reaginic sheep serum, the molecular weight of its heavy chain, its heat lability and long-term skin-sensitizing ability are characteristic of IgE.
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PMID:Isolation and preparation of antisera to ovine IgE. 835 60

We have previously described that normal mouse serum inhibits the PCA reaction mediated by IgE. The present study attempts to characterize this PCA inhibitory factor from the biologically active fraction of the serum. The physicochemical properties of this glycoprotein are the following: it is inactivated at 55 degrees C; it has a molecular weight between 182 kD and 240 kD, determined by gel filtration; it shows affinity to concanavalin A and lentil lectin but not to peanut agglutin; it demonstrates affinity to IgE and, apparently, its carbohydrate moiety is not required for its biological activity. Two bands corresponding to 64.5 kD and 48. 1 kD, which are likely to constitute the biologically active molecule, are observed by SDS-PAGE. These properties are different from those found in factors with IgE affinity involved in IgE synthesis.
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PMID:An anaphylaxis inhibitory factor present in mouse serum. 883 69

Acidobacterium capsulatum is an acid-tolerant, encapsulated, Gram-negative member of the ubiquitous, but poorly understood Acidobacteria phylum. Little is known about the genetics and regulatory mechanisms of A. capsulatum. To begin to address this gap, we identified the gene encoding the A. capsulatum major sigma factor, rpoD, which encodes a 597-amino acid protein with a predicted sequence highly similar to the major sigma factors of Solibacter usitatus Ellin6076 and Geobacter sulfurreducens PCA. Purified hexahistidine-tagged RpoD migrates at approximately 70 kDa under SDS-PAGE conditions, which is consistent with the predicted MW of 69.2 kDa, and the gene product is immunoreactive with monoclonal antibodies specific for either bacterial RpoD proteins or the N-terminal histidine tag. A. capsulatum RpoD restored normal growth to E. coli strain CAG20153 under conditions that prevent expression of the endogenous rpoD. These results indicate we have cloned the gene encoding the A. capsulatum major sigma factor and the gene product is active in E. coli.
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PMID:Identification and characterization of the gene encoding the Acidobacterium capsulatum major sigma factor. 1669 97


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