三种乳酸菌中nadd依赖性甘油醛-3-磷酸脱氢酶的物理生化特性比较

Nina M. Chace , Barbara Sgorbati , Jack London
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引用次数: 0

摘要

对粪链球菌、嗜酸乳杆菌和酿酒Pediococcus cerevisiae中的甘油醛-3-磷酸脱氢酶进行了纯化和表征。这三种酶的分子量分别为135,000、155,000和152,000。这些酶似乎是由四个相同大小的亚基组成,分子量从37,000到42,000不等。初步的抗酿酒酵母甘油醛-3-磷酸脱氢酶血清免疫扩散实验表明,这两种酶具有一定的结构同源性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
A comparison of the physical and biochemical properties of NAD-dependent glyceraldehyde-3-phosphate dehydrogenases from three lactic acid bacteria

The glyceraldehyde-3-phosphate dehydrogenases from Streptococcus faecalis, Lactobacillus acidophilus and Pediococcus cerevisiae were purified to homogeneity and characterized. The respective enzymes exhibit estimated molecular weights of 135,000, 155,000 and 152,000. The enzymes appear to be composed of four subunits of identical size ranging from a molecular weight of 37,000 to 42,000. Preliminary immunodiffusion experiments with anti P. cerevisiae glyceraldehyde-3-phosphate dehydrogenase serum indicate that the enzymes share some degree of structural homology.

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