Hendler E D, Torretti J, Epstein F H
J Clin Invest. 1971 Jun;50(6):1329-37. doi: 10.1172/JCI106612.
The activity of sodium-potassium-activated adenosine triphosphatase (Na-K-ATPase) is considerably higher in homogenates of outer medulla than in the cortex or papilla of the kidney. The enzyme has similar kinetic characteristics in both cortex and medulla, and binds ouabain in the same proportion. The discrepancy in enzymatic activity is not paralleled by similar change in the activity of adenyl cyclase, 5'nucleotidase, glucose-6-phosphatase, or succinic dehydrogenase. Na-K-ATPase is also higher in distal convoluted tubules (ventral slices) than in the proximal tubules (dorsal slices) of the kidney of Amphiuma. The high concentration of Na-K-ATPase in the red medulla of the kidney is probably related to the presence here of the thick ascending limb of the loop of Henle, and this has important implications with regard to the mechanism of sodium reabsorption by different portions of the nephron.
钠钾激活的三磷酸腺苷酶（Na-K-ATP酶）在外髓匀浆中的活性明显高于肾脏皮质或乳头。该酶在皮质和髓质中具有相似的动力学特征，并以相同比例结合哇巴因。腺苷酸环化酶、5'-核苷酸酶、葡萄糖-6-磷酸酶或琥珀酸脱氢酶活性的类似变化并未与酶活性的差异平行。在两栖动物肾脏中，远曲小管（腹侧切片）中的Na-K-ATP酶也高于近曲小管（背侧切片）。肾脏红色髓质中高浓度的Na-K-ATP酶可能与髓袢升支粗段的存在有关，这对肾单位不同部分的钠重吸收机制具有重要意义。
