Sweadner K J
Biochim Biophys Acta. 1978 Apr 20;508(3):486-99. doi: 10.1016/0005-2736(78)90094-9.
A microsomal fraction from canine brain gray matter has been extracted with the detergent sodium dodecyl sulfate to partially purify the membrane-bound (Na+ + K+)-stimulated adenosine triphosphatase. Phospholipid, glycolipid, and a family of other glycoproteins are also enriched by the procedure; it is proposed that the product is an intrinsic membrane protein fraction. 6--8-fold purification of (Na+ + K+)-ATPase is obtained without solubilizing the enzyme and without irreversibly altering its turnover number. Final specific activities are 350--400 mumol of ATP hydrolyzed/h per mg protein. The stimulation and reversible inactivation of the (Na+ + K+)-ATPase by dodecyl sulfate were examined for information relevant to the mechanism of action of the detergent.
已用去污剂十二烷基硫酸钠提取犬脑灰质的微粒体部分，以部分纯化膜结合的（Na⁺ + K⁺）刺激的腺苷三磷酸酶。该过程还富集了磷脂、糖脂和其他一类糖蛋白；有人提出该产物是一种内在膜蛋白部分。在不使酶溶解且不不可逆地改变其周转数的情况下，（Na⁺ + K⁺）-ATP酶得到了6至8倍的纯化。最终的比活性为每毫克蛋白质每小时水解350 - 400 μmol ATP。研究了十二烷基硫酸钠对（Na⁺ + K⁺）-ATP酶的刺激和可逆失活，以获取与去污剂作用机制相关的信息。
