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Purification and Characterization of the Urease Enzymes of Helicobacter Species From Humans and Animals

机译:人和动物中幽门螺杆菌脲酶的纯化与鉴定

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摘要

The urease enzymes of Helicobacter pylori, H. mustelae, H. felis, and H. nemestrinae have been purified to homogeneity by affinity chromatography and characterized. The native urease enzymes of the four organisms were found to be almost identical, with a pI of 6.1 and molecular masses of 480 to 500 kDa, as determined by electrophoretic mobility in nondenaturing polyacrylamide gels. Transmission electron microscopy of the native urease showed it to be a molecule approximately 13 nm in diameter, with hexagonal symmetry. Denaturation studies indicated that each urease enzyme molecule was composed of two nonidentical subunits with molecular masses of approximately 64 and 30 kDa. The subunits were present in a 1:1 ratio, suggesting a hexameric stoichiometry for the native molecule. The predicted molecular mass of H. pylori urease, based on subunit molecular weight and stoichiometry, is 568 kDa. N-terminal amino acid sequencing of the enzyme subunits from the four species revealed high levels of homology. The large subunits (UreB) were found to be 92 to 100% homologous, and the small subunits (UreA) were 75 to 95% homologous over the first 12 to 20 residues. The high degree of homology suggests a common ancestral origin and an important role for the urease enzymes of these organisms.
机译:已通过亲和色谱法将幽门螺杆菌,鼬,H。felis和nemestrinae的脲酶酶纯化至均质并进行了表征。通过非变性聚丙烯酰胺凝胶中的电泳迁移率测定,发现四种生物的天然脲酶几乎相同,pI为6.1,分子量为480至500 kDa。天然脲酶的透射电子显微镜显示它是直径约13 nm的分子,具有六边形对称性。变性研究表明,每个脲酶分子均由两个分子量约64和30 kDa的不同亚基组成。亚基以1:1的比例存在,表明天然分子的六聚体化学计量。基于亚基分子量和化学计量,幽门螺杆菌脲酶的预测分子量为568 kDa。这四个物种的酶亚基的N末端氨基酸测序显示出高水平的同源性。在前12至20个残基中,发现大亚基(UreB)具有92%至100%的同源性,而小亚基(UreA)具有75%至95%的同源性。高度同源性表明这些生物具有共同的祖先起源和重要的作用。

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