贝司他汀抑制[3H]白三烯A4与人类白细胞白三烯A4水解酶的共价偶联。
Bestatin inhibits covalent coupling of [3H]LTA4 to human leukocyte LTA4 hydrolase.
作者信息
Evans J F, Kargman S
机构信息
Department of Pharmacology, Merck Frosst Centre for Therapeutic Research, Pointe Claire-Dorval, Quebec, Canada.
出版信息
FEBS Lett. 1992 Feb 3;297(1-2):139-42. doi: 10.1016/0014-5793(92)80345-h.
The covalent coupling of [3H]LTA4 to human leukocyte LTA4 hydrolase is inhibited in a concentration-dependent fashion by pre-incubation with bestatin. This inhibition correlated with the concentration-dependent inhibition by bestatin of LTB4 and LTB5 synthesis by LTA4 hydrolase. Epibestatin, a diastereomer of bestatin, neither inhibited LTB4 or LTB5 production by LTA4 hydrolase nor prevented the covalent coupling of [3H]LTA4 to the enzyme. In contrast, captopril inhibited both LTB4 synthesis by LTA4 hydrolase and covalent coupling of [3H]LTA4 to the enzyme.
通过与贝司他汀预孵育，[3H]白三烯A4（LTA4）与人白细胞LTA4水解酶的共价偶联以浓度依赖性方式受到抑制。这种抑制作用与贝司他汀对LTA4水解酶合成白三烯B4（LTB4）和白三烯B5（LTB5）的浓度依赖性抑制相关。表贝司他汀是贝司他汀的非对映异构体，它既不抑制LTA4水解酶产生LTB4或LTB5，也不阻止[3H]LTA4与该酶的共价偶联。相比之下，卡托普利既抑制LTA4水解酶合成LTB4，也抑制[3H]LTA4与该酶的共价偶联。
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