Purification of a lipoxygenase from ungerminated barley. Characterization and product formation

P.G.M. Van Aarle; M.M.J. De Barse; G.A. Veldink; J.F.G. Vliegenthart

doi:10.1016/0014-5793(91)80227-T

Purification of a lipoxygenase from ungerminated barley. Characterization and product formation

P.G.M. Van Aarle, M.M.J. De Barse, G.A. Veldink, J.F.G. Vliegenthart

Utrecht University

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

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.

Original language	English
Pages (from-to)	159-162
Number of pages	4
Journal	FEBS Letters
Volume	280
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(91)80227-T
Publication status	Published - 12 Jul 1991

Keywords

Arachidonic acid hydroperoxide
Barley
Linoleic acid hydroperoxide
Lipoxygenase
lipoxygenase
article
barley
enzyme purification
nonhuman
priority journal

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10.1016/0014-5793(91)80227-T

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@article{6930a5e736524f2b96e75725a571f0a7,

title = "Purification of a lipoxygenase from ungerminated barley. Characterization and product formation",

abstract = "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.",

keywords = "Arachidonic acid hydroperoxide, Barley, Linoleic acid hydroperoxide, Lipoxygenase, lipoxygenase, article, barley, enzyme purification, nonhuman, priority journal",

author = "\{Van Aarle\}, P.G.M. and \{De Barse\}, M.M.J. and G.A. Veldink and J.F.G. Vliegenthart",

year = "1991",

month = jul,

day = "12",

doi = "10.1016/0014-5793(91)80227-T",

language = "English",

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journal = "FEBS Letters",

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T1 - Purification of a lipoxygenase from ungerminated barley. Characterization and product formation

AU - Van Aarle, P.G.M.

AU - De Barse, M.M.J.

AU - Veldink, G.A.

AU - Vliegenthart, J.F.G.

PY - 1991/7/12

Y1 - 1991/7/12

N2 - 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.

AB - 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.

KW - Arachidonic acid hydroperoxide

KW - Barley

KW - Linoleic acid hydroperoxide

KW - Lipoxygenase

KW - lipoxygenase

KW - article

KW - barley

KW - enzyme purification

KW - nonhuman

KW - priority journal

U2 - 10.1016/0014-5793(91)80227-T

DO - 10.1016/0014-5793(91)80227-T

M3 - Article

SN - 0014-5793

VL - 280

SP - 159

EP - 162

JO - FEBS Letters

JF - FEBS Letters

IS - 1

ER -

Purification of a lipoxygenase from ungerminated barley. Characterization and product formation

Abstract

Keywords

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