Swanson A A, Davis R M, McDonald J K
Curr Eye Res. 1984 Apr;3(4):659-61. doi: 10.3109/02713688409003068.
A new neutral endopeptidase having the properties of prolyl endopeptidase was detected in bovine lenses. The enzyme hydrolyzed the prolyl bond in the newly-developed fluorogenic substrate, t-butyloxycarbonyl-Arg-Pro-2-NNap, optimally at pH 8 and 37 degrees. The Km value was estimated to be 0.033 mM. An approximately 4-fold purification was achieved. DFP completely inhibited the hydrolysis of Boc-Arg-Pro-2-NNap by the endopeptidase.
在牛晶状体中检测到一种具有脯氨酰内肽酶特性的新型中性内肽酶。该酶在新开发的荧光底物叔丁氧羰基-精氨酸-脯氨酸-2-萘胺中水解脯氨酰键，最适pH为8，温度为37℃。Km值估计为0.033 mM。实现了约4倍的纯化。二异丙基氟磷酸酯完全抑制了该内肽酶对Boc-精氨酸-脯氨酸-2-萘胺的水解。
