• Restorative Dentistry and Endodontics
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• v.8 no.1
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• pp.19-30
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• 1982

This study was performed to elucidate the histopathologic distribution of immunoglobulins, particularly IgA, IgG and IgM in the periapical lesions, including 22 periapical granulomas and 18 periapical cysts. The immunoperoxidase staining method using reagents manufactured and supplied by Danish DAKO company was employed in this study. In comparison with the immunohistochemical methods, this method was proved to be reliable and convinient one to detect immunoglobulins in the tissue. The following results were obtained: 1. In the 22 periapical granulomas, IgG was found in 20 cases (90.9%), IgA in 16 cases (72.7%) and IgM in 19 cases (86.3%). 2. In the 18 periapical cysts, IgG was found in 16 cases (88.8%), IgA in 13 cases (72.2%) and IgM in 15 cases (83.3%). 3. The distribution of immunoglobulins both in periapical granulomas and periapical cysts was in great diversity according to the lesion and area. 4. More immunoglobulins were found in the exudative area with moderate or severe infiltrations of plasma cells and lymphocytes and less concentration of immunoglobulins were seen in the area with leukocytes infiltration and tissue destruction. 5. The area with collagenolysis and reparative activity contained more abundant IgG and IgM than IgA in periapical granulomas. 6. IgG was dominant in the granulomatous connective tissue and immunoglobulins were not easily found in the fibrous capsule in periapical cysts.

• Biotechnology and Bioprocess Engineering:BBE
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• v.6 no.1
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• pp.25-30
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• 2001

Viral safety is a prerequisite for manufacturing clinical albumin and immunoglobulins from human plasma pools. This study was designed to evaluate the efficacy of cold ethanol fractionation and pasteurization (60$\^{C}$ heat treatment for 10h) for the removal/inactivation of human immunodeficiency virus type 1 (HIV-1) during the manufacturing of albumin and immunoglobulins. Samples from the relevant stages of the production process were spiked with HIV-1, and the amount of virus in each fraction was quantified by the 50% tissue culture infectious dose(TCID(sub)50). Both fraction IV fractionation and pasteurization steps during albumin processing were robust and effective in inactivating HIV-1, titers of which were reduced from an initial 8.5 log(sub)10 TCID(sub)50 to undetectable levels. The log reduction factors achieved were $\geq$ 4.5 and $\geq$ 6.5, respectively. In addition, fraction III fractionation and pasteurization during immunoglobulins processing were robust and effective in eliminating HIV-1. HIV-1 titers were reduced from an initial 7.3 log(sub)10 TCID(sub)50 to undetectable levels. The log reduction factors achieved in this case were $\geq$ 4.9 and $\geq$ 5.3, respectively. These results indicate that the process investigated for the production of albumin and immunoglobulins have sufficient HIV-1 reducing capacity to achieve a high margin of safety.

• Korean Journal of Animal Reproduction
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• v.11 no.3
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• pp.181-188
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• 1987

This stduy was carried out to investigate the effects of Isoimmunization by sperm and seminal plasma on density of immunoglobulins in reproductive tract fluids and serum of immunized rabbits. The results obtained were summarized as follows: 1. Antibody titers against sperm and seminal plasma antigen ranged from 8 to 64 to 512, respectively. 2. All immunoglobulins; IgG, IgA and IgM were detected with Indirect ELISA method in the uterine and oviductal fluids as well as the sera of immune rabbits. 3. Concentrations of IgGs in the uterine and oviductal fluids of rabbits immunized with sperm and seminal plasma were higher than those of the control rabbits, but not showed any differences in sera. 4. Amount of IgA in the sera and oviductal fluids of control animals was more than that of the immune animals, while that of IgA in the uterine fluids of control and seminal plasma-immunized animals was higher as compared to sperm immune animals. 5. Average concentration of IgM in the uterine fluids of control and seminal plasma-immunized rabbits was higher than that of sperm-immunized ones. In the oviductal fluids, average concentrations of IgM of immune rabbits was higher than that of immune rabbits.

• Korean Journal of Veterinary Research
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• v.29 no.2
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• pp.75-81
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• 1989

The levels of the serum and colostral total protein and immunoglobulins of the Korean native cows immediately after parturition and colostrum-conferred passive immune status of the Korean native calves were studied, and the results obtained were summerized as follows: The mean total protein, total immunoglobulin, IgG, IgM, and IgA concentrations in sera of 10 Korean native cows immediately after parturition were $6.8{\pm}0.4g/dl$, $24.39{\pm}3.41mg/ml$, $19.49{\pm}2.70mg/ml$, $4.56{\pm}1.14mh/ml$, and $0.35{\pm}0.08mg/ml$ respectively. And the mean total protein, total immunoglobulin, IgG, IgM, and IgA concentrations in colostrum were $15.0{\pm}1.1g/dl$, $116.13{\pm}23.07mg/ml$, $101.51{\pm}22.59mg/ml$, $9.46{\pm}1.99mg/ml$, and $5.17{\pm}1.59mg/ml$ respectively. The mean concentrations of total protein and immunoglobulins in colostrum were 2.1 times to 14.8 times higher than those in serum. The mean concentrations of total protein, total immunoglobuln, IgG, IgM, and IgA in sera from 211 Korean native calves at 2 days old were $6.7{\pm}0.9g/dl$, $35.74{\pm}9.56mg/ml$, $29.06{\pm}8.07mg/ml$, $4.91{\pm}2.99mg/ml$, and $1,9{\pm}0.99mg/ml$ respectively. Although the calves had been suckled the dam's colostrum, each of calves was considerably various in levels of serum total protein and immunoglobulins and 16.1 percent of the calves were in a state of hypoglobulinemia.

• Korean journal of food and cookery science
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• v.12 no.1
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• pp.54-59
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• 1996

Immunoglobulins (IgY) were isolated from egg yolk of hens immunized with bovine serum albumin(BSA). The stability of anti-BSA IgY against heat and pH was investigated. Antibody activity was measured by enzyme linked immunosorbent assay. IgY was relatively heat-stable and most of the antibody activity remained after heating up 65$^{\circ}C$ for 30 minutes. IgY was stable at pH 5-11. However, inactivation of IgY was observed below pH 4, or above pH 12. Inactivation of IgY proceeded rapidly at low pHs(pH 2-3). Most of the antigen binding activity was lost at low pHs probably because of some conformational changes.

• Parasites, Hosts and Diseases
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• v.40 no.2
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• pp.93-99
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• 2002

The effect of a secretory proteinase from the pathogenic amoebae Acanthamoeba castellanii on host's defense-oriented or regulatory proteins such as immunoglobulins, interleukin-1, and protease inhibitors was investigated. The enzyme was found to degrade secretory immunoglobulin A (slgA), IgG, and IgM. It also degraded $interleukin-1{\alpha}$ ($IL-l{\alpha}$) and $IL-l{\beta}$. Its activity was not inhibited by endogenous protease inhibitors, such as ${\alpha}$2-macroglobulin, ${\alpha}l-trypsin$ inhibitor, and ${\alpha}2-antiplasmin$. Furthermore, the enzyme rapidly degraded those endogenous protease inhibitors as well. The degradation of host's defense-oriented or regulatory proteins by the Acanthanoeba proteinase suggested that the enzyme might be an important virulence factor in the pathogenesis of Acanthamoeba infection.

• Journal of Microbiology
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• v.34 no.1
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• pp.95-100
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• 1996

The effect of the extracellular protease of Salmonella schottmulleri on human serum constituents such as immunoglobulins, hemoglobin and lysozyme and tissue constituents such as fibronectin and collagens was investigated. This protease degraded collagens (type I and III), fibronectin and serum proteins such as human hemoglobin and lysozyme. Bovine serum albumin was degraded slightly. Thus, the present study suggested the possibility that this protease is not only played an important role in invasion of S. schottmulleri by degrading the constituent proteins such as collagens and fibronectin but also induced complications observed in septicemia and chronic infections by degrading the serum proteins. This protease is also capable of degrading defence-oriented humoral proteins, immunoglobulins (IgG and IgM). Furthermore, it is toxic to HEp-2 cells. These findings clarified the possible role of Salmonella protease as a virulence factor in the pathogenesis of Salmonella infections.

• Parasites, Hosts and Diseases
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• v.35 no.1
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• pp.39-46
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• 1997

The present study was undertaken to determine whether live T. uaginnlis degrades human secretory IgA, serum If and IgG molecules. Human immunoglobulins were exposed to live trophozoites, parasite Iysate, and excretory-secretory product (ESP) of T ucginnlis. To determine the fragmentation of immunoglobulins, the reaction sample was subjected to SDS-PAGE and EITB, and peroxidase conjugated antihuman IgA and IgG were used as probes. Live trophozoites degraded secretory IgA, serum IgA and IgG, and degradation were pressed forward by the prolongation of the incubation time and by increasing the number of trichomonads respectively. Also the Iysates and ESP of trichomonads degraded IgA and IgG. The cysteine and serine proteinase inhibitors such as I-64, antipain, iodoacetic acid, iodoacetamide, TLCK reduced the ability of cleaving immunoglobulins. The proteinase activity and cytotoxicity of T. uaginnlis to HeLa cells were decreased when live T. vusinalis was treated with metallo-proteinase inhibitor as well as cysteine and serine proteinase inhibitors. These results suggest that proteinase secreted from live T ucginclis may play a part role in host pathogenesis by T. uosinnlis, and the cleaving ability of host immunoglobulins by the proteinase may contribute as a one of immune evasion mechanism for parasite survival in the host.

• Journal of the korean veterinary medical association
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• v.30 no.11
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• pp.671-678
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• 1994

• Journal of the korean veterinary medical association
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• v.30 no.8
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• pp.454-465
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• 1994