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Characterization of neuraminidases produced by various serotypes of Pasteurella multocida.

机译:表征由多种血清型多杀巴斯德氏菌产生的神经氨酸酶。

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Neuraminidases produced by 16 strains of Pasteurella multocida (serotypes 1 to 16) were characterized by molecular weight, substrate specificity, and antigenic identity. After growth in a chemically defined medium, stage I (lyophilized) culture supernatants were assayed for activity with N-acetylneuramin lactose, human alpha-1-acid glycoprotein, fetuin, colominic acid, and bovine submaxillary mucin. Neuraminidase produced by P. multocida A:3 was purified by a combination of salt fractionation, ion-exchange chromatography on DEAE-Sephacel, and gel filtration on Sephadex G-200. Purified P. multocida A:3 neuraminidase was employed to immunize rabbits, and the resulting antiserum reduced the activity of the P. multocida A:3 enzyme by 40.3%. This antiserum also reduced the activities of the neuraminidases produced by other serotypes by between 30.8 and 59.6%. Molecular weight estimates of the neuraminidases produced by the various serotypes were obtained by gel filtration chromatography on Sephadex G-200. Each of the 16 serotypes examined produced a neuraminidase with a molecular weight of approximately 500,000. In addition, all 16 high-molecular-weight neuraminidases showed similar substrate specificities. On the basis of these data, it appears that the high-molecular-weight neuraminidases produced by different P. multocida serotypes are quite similar.
机译:通过分子量,底物特异性和抗原同一性来表征由16个多杀巴斯德氏菌菌株(1至16型)产生的神经氨酸酶。在化学成分确定的培养基中生长后,用N-乙酰神经氨酸乳糖,人α-1-酸糖蛋白,胎球蛋白,结肠酸和牛下颌黏液测定I期(冻干)培养上清液的活性。通过盐分馏,DEAE-Sephacel上的离子交换色谱和Sephadex G-200上的凝胶过滤的组合纯化由P. multocida A:3产生的神经氨酸酶。使用纯化的多杀疟原虫A:3神经氨酸酶免疫兔,所得抗血清使多杀疟原虫A:3酶的活性降低40.3%。该抗血清还将其他血清型产生的神经氨酸酶的活性降低了30.8%至59.6%。在Sephadex G-200上通过凝胶过滤色谱法获得了由各种血清型产生的神经氨酸酶的分子量估计。检查的16种血清型中的每一种均产生了分子量约为500,000的神经氨酸酶。此外,所有16种高分子量神经氨酸酶均显示相似的底物特异性。根据这些数据,似乎由不同的多杀毕赤氏酵母血清型产生的高分子量神经氨酸酶非常相似。

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