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首页> 外文期刊>Journal of bacteriology >Purification and properties of streptococcal nicotinamide adenine dinucleotide glycohydrolase.
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Purification and properties of streptococcal nicotinamide adenine dinucleotide glycohydrolase.

机译：链球菌烟酰胺腺嘌呤二核苷酸糖水解酶的纯化和性质。

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摘要

Highly purified streptococcal nicotinamide adenine dinucleotide glycohydrolase (NADase) was obtained by utilizing disodium tetrathionate to protect the enzyme by blocking the sulfhydryl groups of streptococcal proteinase. This was followed by two-step ion-exchange chromatography. The pure enzyme, demonstrated as a single band on sodium dodecyl sulfate/polyacrylamide gel electrophoresis, had a specific activity of 11,200 NADase units per mg of protein and was devoid of hemolytic activity. NADase had a molecular weight of about 55,000 as determined by gel filtration, by summation of amino acid residues, and by sodium dodecyl sulfate/gel electrophoresis. The purified enzyme had optimal activity at pH 7.3 and at 40 C and a calculated Km of 5.1 times 10- minus 4 mM. It was inhibited by alpha-iodoacetamide.
机译：通过利用四硫代硫酸钠来封闭链球菌蛋白酶的巯基来保护该酶，从而获得了高纯度的链球菌烟酰胺腺嘌呤二核苷酸糖水解酶。随后进行两步离子交换色谱。该纯酶在十二烷基硫酸钠/聚丙烯酰胺凝胶电泳上显示为单条带，比活性为11,200 NADase单位/ mg蛋白质，并且没有溶血活性。通过凝胶过滤，氨基酸残基的总和以及十二烷基硫酸钠/凝胶电泳测定，NADase的分子量约为55,000。纯化的酶在pH 7.3和40°C时具有最佳活性，计算的Km为5.1乘10减去4 mM。它被α-碘乙酰胺抑制。

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