Optimization of cofactors which regulate RBL-1 arachidonate 5-lipoxygenase.

Abstract:

:The arachidonate lipoxygenase from rat basophilic leukemia cells (RBL-1) is widely utilized as a model to dissect the primary enzymatic reactions leading to leukotriene formation. The purpose of the present study was to optimize the specific activity of 5-lipoxygenase prepared from a high speed supernatant of RBL-1 cell homogenates. Activation of 5-lipoxygenase was observed in the presence of micromolar levels of calcium. A synergistic enhancement of 5-lipoxygenase was observed upon addition of equally low levels of ATP; maximal activation was induced by 5 microM CaCl2 plus 5 microM ATP. Addition of a microsomal-membrane preparation and NADPH further augmented 5-HETE biosynthesis. High concentrations (330 microM) of NADPH reversed the microsomal-induced stimulation of RBL-1 5-lipoxygenase, resulting in enzyme inhibition.

authors

Cochran FR,Finch-Arietta MB

doi

10.1016/0006-291x(89)91388-0

subject

Has Abstract

pub_date

1989-06-30 00:00:00

pages

1327-32

issue

3

eissn

0006-291X

issn

1090-2104

pii

0006-291X(89)91388-0

journal_volume

161

pub_type

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