• Restorative Dentistry and Endodontics
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• 제8권1호
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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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• 제6권1호
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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.

• 한국가축번식학회지
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• 제11권3호
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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.

• 대한수의학회지
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• 제29권2호
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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.

• 한국식품조리과학회지
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• 제12권1호
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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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• 제40권2호
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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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• 제34권1호
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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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• 제35권1호
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• pp.39-46
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• 1997

이 연구에서는 살아있는 질편모충의 단백질녈해효소가 인체 면역글로불린을 분해하는지 알아보고 질편모충에 의한 조직세포 독성에 있어서 단백질분해효소의 역할을 시험관내에서 관찰하였다 실험에 사용한 질편모충은 질염환자로년터 분리한 KT9 분리주이었으며 세포독성을 알아보기 위한 표적세포로는 HeLa 세포를 사용하였다 질편모충 단백질분해효소가 인체 면역글로불린을 분해하는지 관찰하고자 인체의 분비 IP. 혈청 IgA 및 IgG를 살아있는 원충. 원충의 용출액 및 분비-배설 액과 DTT를 넣어 반응시켰다. 여러 계열의 단백질분해효소 저해제(aminopeptidase, serine, metallo, cystelrle계열)를 살아있는 질편모충과 미리 반응시킨 후 세척하고 면역글로불린의 분해 단백질분해효소 활성 및 조직세포독성에 미치는 영향을 관찰하였다 살아있는 질편모충은 인체의 분비 IgA. 혈청 IgA 및 IgG를 분해하였는데 질편모충 수가 증가할수록 반응시간이 길수록 분해가 더 잘 이루어졌다 질푄모충의 용출액과 분비-배설액도 분비 IgA. 혈청 IgA 및 IgG를 분해하였다. Cysteine, serine계 열의 단백질분해효소 저해제 (I-64 antipain, iodoacetic acid, iodoacetamide, TLCK)를 처리한 질편닐충은 분비 IgA의 분해를 저해하였으며. 단백질분해효소저해제로 처리한 경우 질편모충의 단백질븐해효소 활성은 감소하였고 HeLa세포에 대한 독성이 감소하였다. 이상의 성적을 종합하면 질편모충에서 분비되는 단백질분해효소는 시험관내에서 조직세포에 세포독성을 나타내며 또한 인체면역글로불린을 분해하여 숙주의 방어기전에 대한 도피물질로 작용하는 것으로 생각된다.

• 대한수의사회지
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• 제30권11호
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• pp.671-678
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• 1994

• 대한수의사회지
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• 제30권8호
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• pp.454-465
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• 1994