Purification of a lipoxygenase from ungerminated barley Characterization and product formation

FEBS Letters

Veldink, Gerrit A.¹  Vliegenthart, Johannes F.G.¹  de Barse, Martina M.J.¹  van Aarle, Peter G.M.¹ 

[1] Bijvoet Center for Biomolecular Research, Department of Bio-Organic Chemistry, Utrecht University, Utrecht, The Netherlands

关键词: Lipoxygenase;    Linoleic acid hydroperoxide;    Arachidonic acid hydroperoxide;    Barley;   

DOI  :  10.1016/0014-5793(91)80227-T

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 (9S)-(10E,12Z)-9-hydroperoxy-10, 12-octadecadienoic acid, and arachidonic acid into (5S)-(6E,8Z,11Z,14Z)-5-hydroperoxy-6,8,11,14-cicosatetraenoic acid.

【 授权许可】

Unknown