Open AccessSelf‐Inactivation by 13‐Hydroperoxylinoleic Acid and Lipohydroperoxidase Activity of the Reticulocyte Lipoxygenase
Author(s) -
HÄRTEL Brigitte,
LUDWIG Peter,
SCHEWE Tankred,
RAPOPORT Samuel M.
Publication year - 1982
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1982.tb06787.x
Subject(s) - reticulocyte , chemistry , lipoxygenase , linoleic acid , sodium borohydride , biochemistry , ferrous , ferric , enzyme , organic chemistry , fatty acid , catalysis , messenger rna , gene
1 The self‐inactivation of lipoxygenase from rabbit reticulocytes with linoleic acid at 37°C is caused by the product 13‐hydroperoxylinoleic acid. This inactivation is promoted by either oxygen or linoleic acid. 2 Lipohydroperoxidase activity was demonstrated with 13‐hydroperoxylinoleic acid plus linoleic acid as hydrogen donor under anaerobic conditions at 2°C. The products were 13‐hydroxylinoleic acid, oxodienes and compounds of non‐diene structure similar to those produced by soybean lipoxygenase‐1. 3 13‐Hydroperoxylinoleic acid also changed the absorbance and fluorescence properties of reticulocyte lipoxygenase. The results indicate that one equivalent of 13‐hydroperoxylinoleic acid converts the enzyme from the ferrous state into the ferric state as described for soybean lipoxygenase‐1. The spectral changes were reversed by sodium borohydride at 2°C, but not at 37°C; it is assumed that the ferric form of reticulocyte lipoxygenase suffers inactivation.