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NAOSITE : Nagasaki University's Academic Output SITE > Institute of Tropical Medicine > Bulletin > Tropical medicine > Volume 14, No. 3 >

ウェステルマン肺吸虫の抗原分析に関する研究 : 1.成虫体抽出液の抗原活性と理化学的性状に及ぼす加熱の影響


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Title: ウェステルマン肺吸虫の抗原分析に関する研究 : 1.成虫体抽出液の抗原活性と理化学的性状に及ぼす加熱の影響
Other Titles: Studies on the Antigenic Analysis in paragonimus westermani : 1. Effect of Heating upon the Serological Activity and Physico-chemical Character of the Adult-worm Extract
Authors: 今井, 淳一
Authors (alternative): Imai, Jun-Ichi
Issue Date: 30-Sep-1972
Publisher: 長崎大学熱帯医学研究所 / Institute of Tropical Medicine, Nagasaki University
Citation: 熱帯医学 Tropical medicine 14(3). p111-123, 1972
Abstract: An antigen which was extracted in saline from the adult worm of Paragonimus westermani was treated by heating at differed degrees of temperature. Examination was made on the serological activity of these antigens and on the physico-chemical character of their protein components. In this study, use was done of the sera taken from paragonimiasis patients, experimentally infected cats and immunized rabbits. The agar-gel diffusion test and the complement fixation were employed for immunological measurement and the polyacrylamide-gel electrophoresis was done for protein determination. (1) The total protein quantity in the antigen was found to decrease in inverse proportion to the height of temperature for heating. For example, approximately 30% of protein was coagulated by heating at 100℃ for 10 minutes. While, change of the carbohydrate quantity was very little and only 3.2% of it was lost by the same treatment. (2) In the findings of the electrophoretic pattern, the protein components to move rapidly to the anoden side appeared to be lost by raising the heating-temperature and these components were contained in the ES (excretion and secretion) antigen. On the other hand, the bands to move slowly to the cathoden side appeared to be almost unchanged or slightly decreased in quantity by heating. From this finding, these components were thought to be rather thermostable. The quantity of these ones in the ES antigen was very little. (3) The heated antigens were examined on their serological characteristics to 6 of the infected cat sera and 22 of the patient sera by the agar-gel diffusion test. The somatic antigen heated at 60℃ for 10 minutes showed precipitin lines to all the sera employed. The one heated at 70℃, however, showed a negative result to 6 of the patient sera. Further, with the one done at 80℃ or more, the reaction changed to negative to all the sera except 2 of the infected cat ones. To the immunized rabbit sera, precipitin lines were observed even by the antigen heated at 100℃. The increase of the heating-time from 5 up to 30 minutes resulted in the disappearance of the fine and weak precipitin lines but little was influenced on the formation of the main precipitin lines. (4) In the complement fixation, the dilution-titre of the antisarum showing a positive reaction to the heated antigen became lower by raising the heating-temperature. To antisera of high concentration, the heated antigen showed a positive reaction even with the dilution of 6,400 to 12,800 times. It was estimated that in the complement fixation, there were two reaction systems which were given separately by the thermostable antigen fractions and thermolabile ones. / 1)虫体抽出液の可溶性蛋白質は比較的耐熱性のものが多く,100℃,10min.の加熱で全体の約30%が凝固沈澱した.にれに比べ糖類は更に安定で100℃加熱でも約3%が減少したにすぎない。2)加熱処理による虫体抗原の紫外線吸収の変化は加熱温度の上昇に併行して吸収帯は顕著となる。その吸収帯は250~260mμに認められる。これに対しES抗原は280mμに吸収帯を認め,虫体抗原と質的な相違がみられる.3)虫体抗原の電気泳動像は陽極域に速やかに移動する成分と陰極で殆んど移動しない成分に大別され,前者は加熱温度の増大と共に泳動帯が順次消失し,後者は加熱に対して影響が少なく耐熱性を示した.易熱性成分の多くはES抗原に認められ,80℃,10min.処理でその殆んどが破壊される。4)血清学的活性,沈降反応による変化は理化学的性状の変化と概ね平行関係が認められる.感染血清に対しては80℃加熱で沈降反応活性の失活がみられる。これに対し虫体抗原で感作した家兎血清に対する反応では100℃加熱でも活性の保持が認められた。5)補体結合反応による感作抗血清に対する加熱抗原の活性変化は加熱温度が上昇するに従い陽性反応を呈する抗血清の希釈倍数は著しく低下する。然し濃度の高い抗血清では熱処理された抗原でも高い抗原希釈倍数で尚活性が認められた.
URI: http://hdl.handle.net/10069/4117
ISSN: 03855643
Type: Departmental Bulletin Paper
Appears in Collections:Volume 14, No. 3

Citable URI : http://hdl.handle.net/10069/4117

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