Nω-Allyl-l-arginine is shown to be a competitive reversible inhibitor and time-dependent inactivator of bovine brain nitric oxide synthase (nNOS). The enzyme is protected against inactivation by the presence of the substrate, the absence of O2, or if NADP+ is substituted for NADPH. The NADPH absorption spectrum is converted to that of NADP+ concomitant with inactivation. The latter two results indicate that
Nω-烯丙基-l-精
氨酸被证明是牛脑
一氧化氮合酶 (nNOS) 的竞争性可逆
抑制剂和时间依赖性灭活剂。底物的存在、O2 的不存在或
NADP+ 被
NADPH 取代,可保护酶免于失活。
NADPH 吸收光谱被转换为伴随失活的
NADP+ 吸收光谱。后两个结果表明灭活需要氧化还原
化学。Nω-烯丙基-Nω-羟基-l-精
氨酸被合成并显示为nNOS的竞争性
抑制剂和时间依赖性灭活剂,表明它是灭活过程中的可行中间体。用 Nω-烯丙基-[14C]-l-精
氨酸或 Nω-[3H] 烯丙基-l-精
氨酸灭活 nNOS,然后进行凝胶过滤或透析,不会导致与酶结合的放射性。分光光度法和 HPLC 显示血红素在灭活过程中被修饰为四种不同的物种。电感耦合等离子体原子发射分光光度法是...