Solubilization and characterization of the leukotriene C4 synthetase of rat basophil leukemia cells: a novel, particulate glutathione S-transferase.
Solubilization and characterization of the leukotriene C4 synthetase of rat basophil leukemia cells: a novel, particulate glutathione S-transferase.
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大鼠嗜碱性粒细胞白血病细胞白三烯 C4 合成酶的溶解和表征:一种新型颗粒谷胱甘肽 S-转移酶。
DOI:
10.1016/0003-9861(84)90426-0
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发表时间:
1984
影响因子:
3.9
通讯作者:
D. R. Morton
中科院分区:
文献类型:
--
作者:
M. K. Bach;J. R. Brashler;D. R. Morton
Rat basophil leukemia cell homogenates effectively catalyze the conversion of leukotriene A4to a mixture of leukotrienes C4and D4in the presence of glutathione. These homogenates also catalyze the formation of adducts of halogenated nitrobenzene with glutathione, as determined spectrophotometrically. While all the classical glutathioneS-transferase activity resides in the soluble fraction of the homogenates, the thiol ether leukotriene-generating activity is found in the particulate fraction. This “leukotriene C synthetase” activity has been solubilized from a crude high-speed particulate fraction by means of the nonionic detergent, Triton X-100. The solubilized enzyme is incapable of converting 2,4-dinitrochlorobenzene to a colored product in the presence of glutathione. Nor will it react with 3,4-dichloronitrobenzene. On the other hand, under optimal conditions, this enzyme preparation is capable of generating about 0.1 nmol leukotriene C mg protein−1min−1in a reaction which continues in linear fashion for at least 10 min. This dissociation in substrate specificity, as well as differences in the inhibition profile, distinguish the enzyme activity in the particulate fraction from rat basophil leukemia cell homogenates from the microsomal glutathioneS-transferase which has been described in rat liver homogenates, suggesting that this “leukotriene C synthetase” is a new and unique enzyme.
DOI:
--
发表时间:
1982
期刊:
European journal of biochemistry / FEBS
影响因子:
--
作者:
Morgenstern,R;Guthenberg,C;Depierre,JW
通讯作者:
Depierre,JW