Rybák M, Kasafírek E, Rybáková B, Simonianová E
Experientia. 1979 Aug 15;35(8):996-7. doi: 10.1007/BF01949902.
The use of dipeptide-p-nitranilides for the study of 2 placental aminopeptidases separated on Sephadex G200 helped in establishing some regular features of their specifities. The high-molecular (320,000 daltons) one prefers Phe in position P'1 to Leu, whereas the lower-molecular aminopeptidase (145,000 daltons) prefers Leu. The high-molecular aminopeptidase splits very slowly the N-terminal Leu when Gly is in adjacent position. Leu-Gly-p-NA is therefore an inhibitor of this AP.
利用二肽对硝基苯胺研究在Sephadex G200上分离出的两种胎盘氨基肽酶,有助于确定其特异性的一些规律特征。高分子量(320,000道尔顿)的那种在P'1位置更倾向于苯丙氨酸而非亮氨酸,而低分子量的氨基肽酶(145,000道尔顿)则更倾向于亮氨酸。当甘氨酸处于相邻位置时,高分子量氨基肽酶对N端亮氨酸的切割非常缓慢。因此,亮氨酰 - 甘氨酰 - 对硝基苯胺是这种氨基肽酶的抑制剂。