Stewart D J, Semply E W, Swart G T, Sen A K
Biochim Biophys Acta. 1976 Jan 8;419(1):150-63. doi: 10.1016/0005-2736(76)90379-5.
The (Na+ plus K+)-ATPase activities in salt gland homogenates increased 3- to 4-fold after saline treatment of ducks for 3 weeks. The ATPase was purified to a specific activity of 460 and 1015 mumol Pi/mg protein per h, respectively, in control and saline-treated ducks. The catalytic protein was identified on polyacrylamide electrophoresis gels by phosphorylating the enzyme with (32P)ATP. The molecular weight of the protein was estimated to be 98 000. The amount of catalytic unit increased commensurately with the enzyme activity after saline treatment. It is therefore concluded that the increased enzyme activity is due to a de novo enzyme synthesis and is not an activation effect. Phospholipid concentration in the salt gland tissue increased 1.7-fold after the saline treatment. Significant increases occurred in the percentage of the total phospholipids as phosphatidylserine and sphingomyelin. In the partially purified (Na+ plus K+)-ATPase preparation, the percentage composition of phosphatidylserine and phosphatidylethanolamine increased after saline treatment.
用盐水处理鸭子3周后，盐腺匀浆中的（钠+钾）-ATP酶活性增加了3至4倍。在对照鸭和盐水处理的鸭中，ATP酶分别被纯化至每小时460和1015微摩尔无机磷/毫克蛋白质的比活性。通过用（32P）ATP使酶磷酸化，在聚丙烯酰胺电泳凝胶上鉴定出催化蛋白。该蛋白的分子量估计为98000。盐水处理后，催化单位的量与酶活性相应增加。因此得出结论，酶活性的增加是由于从头合成酶，而不是激活作用。盐水处理后，盐腺组织中的磷脂浓度增加了1.7倍。作为磷脂酰丝氨酸和鞘磷脂的总磷脂百分比显著增加。在部分纯化的（钠+钾）-ATP酶制剂中，盐水处理后磷脂酰丝氨酸和磷脂酰乙醇胺的百分比组成增加。
