Premium
Purification of a lipoxygenase from ungerminated barley Characterization and product formation
Author(s) -
van Aarle Peter G.M.,
de Barse Martina M.J.,
Veldink Gerrit A.,
Vliegenthart Johannes F.G.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80227-t
Subject(s) - lipoxygenase , polyclonal antibodies , enzyme , antiserum , biochemistry , arachidonic acid , molecular mass , western blot , chemistry , arachidonate 5 lipoxygenase , biology , antibody , gene , immunology
Lipoxygenase was purified from ungerminated barley (variety ‘Triumph’), yielding an active enzyme with a pl of 5.2 and a molecular mass of approximately 90 kDa. In addition to the 90 kDa band SDS‐PAGE showed the presence of two further proteins of 63 kDa. Western blot analysis showed cross‐reactivity of each of these proteins with polyclonal antisera against lipoxygenases from pea as well as from soybean, suggesting a close immunological relationship. he 63 kDa proteins appear to be inactive degradation products of the active 90‐kDa enzyme. This barley lipoxygenase converts linolcic acid mainly into (9 S )‐(10 E ,12 Z )‐9‐hydroperoxy‐10, 12‐octadecadienoic acid, and arachidonic acid into (5 S )‐(6 E ,8 Z ,11 Z ,14Z)‐5‐hydroperoxy‐6,8,11,14‐cicosatetraenoic acid.