Puscas I, Coltau M
Romanian Academy, Center for Medical Research and Assistance, Simleu Silvaniei, Salaj.
Arzneimittelforschung. 1995 Aug;45(8):846-8.
The aim of the present study was to follow the effect of nitric oxide (NO) on carbonic anhydrase in vitro and in vivo. The effect of L-arginine (as source of NO), as well as that of its analogue, nitro-G-monomethyl-L-arginine, an inhibitor of NO synthesis on carbonic anhydrase, were also studied. In vitro results showed that L-arginine activates carbonic anhydrase, while N-G-monomethyl-L-arginine does not modify its activity. In vivo, L-arginine and N-G-monomethyl-L-arginine increased carbonic anhydrase activity by 72% and, 160% respectively. Administration of L-arginine, as a source of NO, and of acetazolamide before administration of N-G-monomethyl-L-arginine abolished the activating effect of the analogue on carbonic anhydrase. These results lead to the conclusion that inhibition of NO synthesis by N-G-monomethyl-L-arginine induces increase of carbonic anhydrase activity. The data also suggest that NO biosynthetized from L-arginine inhibits carbonic anhydrase.
本研究的目的是在体外和体内追踪一氧化氮（NO）对碳酸酐酶的影响。同时还研究了L-精氨酸（作为NO的来源）及其类似物硝基-G-单甲基-L-精氨酸（一种NO合成抑制剂）对碳酸酐酶的影响。体外实验结果表明，L-精氨酸可激活碳酸酐酶，而N-单甲基-L-精氨酸不会改变其活性。在体内，L-精氨酸和N-单甲基-L-精氨酸分别使碳酸酐酶活性提高了72%和160%。在给予N-单甲基-L-精氨酸之前，先给予作为NO来源的L-精氨酸和乙酰唑胺，可消除该类似物对碳酸酐酶的激活作用。这些结果得出结论：N-单甲基-L-精氨酸对NO合成的抑制会导致碳酸酐酶活性增加。数据还表明，由L-精氨酸生物合成的NO会抑制碳酸酐酶。
