Ray K, Harris H
FEBS Lett. 1986 Jan 1;194(1):91-5. doi: 10.1016/0014-5793(86)80057-6.
A neutral endopeptidase (EC 3.4.24.5) previously thought to be unique to the eye lens has been found to be closely similar if not identical in native molecular size, component polypeptides and antigenic structure to a neutral proteinase from pituitary. Here we investigated some subtle differences in properties of the two enzymes, such as the effects of temperature, divalent cations and SDS on their activities with respect to different substrates. We conclude that the pituitary enzyme may have a relatively more compact structure requiring relaxation by low SDS concentration or higher temperature for maximum activity.
一种先前被认为是晶状体所特有的中性内肽酶（EC 3.4.24.5），现已发现其在天然分子大小、组成多肽和抗原结构方面，即便与垂体来源的中性蛋白酶不完全相同，也极为相似。在此，我们研究了这两种酶在性质上的一些细微差异，例如温度、二价阳离子和SDS对它们针对不同底物的活性的影响。我们得出结论，垂体酶可能具有相对更紧密的结构，需要低浓度SDS或更高温度使其松弛以达到最大活性。
