Bondiou M T, Bourbouze R, Bernard M, Percheron F, Perez-Gonzalez N, Cabezas J A
Clin Chim Acta. 1985 Jun 30;149(1):67-73. doi: 10.1016/0009-8981(85)90274-8.
A urinary fraction which inhibits the activity of N-acetyl-beta-D-glucosaminidase (NAG) has been isolated and identified as being urea. Usually present in high concentration, urea appears to be the only urinary component responsible for the frequently observed urinary NAG inhibition. The inhibition of the two urinary NAG isoenzymes A and B is competitive with respective Ki values of about 70 mmol/l and 60 mmol/l. With routine assay conditions, it seems that a dilution of urine prior to enzyme assay is sufficient to abolish the inhibition of the two isoenzymes A and B by endogenous urea.
一种能抑制N-乙酰-β-D-氨基葡萄糖苷酶(NAG)活性的尿液成分已被分离出来并鉴定为尿素。尿素通常以高浓度存在,似乎是导致经常观察到的尿液NAG抑制现象的唯一尿液成分。对两种尿液NAG同工酶A和B的抑制是竞争性的,其各自的Ki值约为70 mmol/l和60 mmol/l。在常规测定条件下,似乎在酶测定前对尿液进行稀释就足以消除内源性尿素对两种同工酶A和B的抑制作用。