PURIFICATION OF A LIPOXYGENASE FROM UNGERMINATED BARLEY - CHARACTERIZATION AND PRODUCT FORMATION

被引：61

作者：

VANAARLE, PGM ^{[1
]}

DEBARSE, MMJ ^{[1
]}

VELDINK, GA ^{[1
]}

VLIEGENTHART, JFG ^{[1
]}

机构：

[1] STATE UNIV UTRECHT, BIJVOET CTR BIOMOLEC RES, DEPT BIOORGAN CHEM, POB 80075, 3508 TB UTRECHT, NETHERLANDS

来源：

FEBS LETTERS | 1991年 / 280卷 / 01期

关键词：

LIPOXYGENASE; LINOLEIC ACID HYDROPEROXIDE; ARACHIDONIC ACID HYDROPEROXIDE; BARLEY;

D O I：

10.1016/0014-5793(91)80227-T

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Lipoxygenase was purified from ungerminated barley (variety 'Triumph'), yielding an active enzyme with a pI 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. The 63 kDa proteins appear to be inactive degradation products of the active 90-kDa enzyme. This barley lipoxygenase converts linoleic 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-eicosatetraenoic acid.

引用

页码：159 / 162

页数：4

共 29 条

[1] LIPOXIDASES IN MALTING AND MASHING [J].