BESTATIN INHIBITS COVALENT COUPLING OF [H-3] LTA4 TO HUMAN-LEUKOCYTE LTA4 HYDROLASE

被引：26

作者：

EVANS, JF

KARGMAN, S

机构：

[1] Department of Pharmacology, Merck Frosst Centre for Therapeutic Research, Pointe Claire-Dorval, Que.

来源：

FEBS LETTERS | 1992年 / 297卷 / 1-2期

关键词：

LTA4; HYDROLASE; BESTATIN; H-3]LTA4 COVALENT COUPLING; HUMAN LEUKOCYTE;

D O I：

10.1016/0014-5793(92)80345-H

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The covalent coupling of [H-3]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 [H-3]LTA4 to the enzyme. In contrast, captopril inhibited both LTB4 synthesis by LTA4 hydrolase and covalent coupling of [H-3]LTA4 to the enzyme.

引用

页码：139 / 142

页数：4

共 23 条

[1]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[2]

EVANS JF, 1985, J BIOL CHEM, V260, P966

[3] PURIFICATION AND CHARACTERIZATION OF LEUKOTRIENE-A4 HYDROLASE FROM RAT NEUTROPHILS [J].