Lipoxygenase in fish tissue: Some properties of the 12-lipoxygenase from trout gill

Rudolf J. Hsieh; J. Bruce German; John E. Kinsella

Lipoxygenase in fish tissue: Some properties of the 12-lipoxygenase from trout gill

Rudolf J. Hsieh, J. Bruce German, John E. Kinsella

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

Abstract

The gill and skin tissues from several fish species contain active lipoxygenase, which is capable of oxidizing polyunsaturated fatty acids into hydroperoxides. Gill lipoxygenase of rainbow trout exhibited similar reactivities toward arachidonic, eicosapentaenoic, and docosahexaenoic acids, but low reactivity toward linoleic acid. The lipoxygenase exhibited activity from pH 7 to 9 with optimum pH at 7.5. The enzyme was rapidly inactivated at temperatures above 40°C. Stability of gill lipoxygenase was enhanced in the presence of glutathione. Inactivation of lipoxygenase by sulfhydryl-specific reagents suggested that thiol groups were involved in its activity.

Original language	English (US)
Pages (from-to)	680-685
Number of pages	6
Journal	Journal of Agricultural and Food Chemistry
Volume	36
Issue number	4
State	Published - 1988
Externally published	Yes

ASJC Scopus subject areas

Agricultural and Biological Sciences (miscellaneous)
Food Science
Chemistry (miscellaneous)

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title = "Lipoxygenase in fish tissue: Some properties of the 12-lipoxygenase from trout gill",

abstract = "The gill and skin tissues from several fish species contain active lipoxygenase, which is capable of oxidizing polyunsaturated fatty acids into hydroperoxides. Gill lipoxygenase of rainbow trout exhibited similar reactivities toward arachidonic, eicosapentaenoic, and docosahexaenoic acids, but low reactivity toward linoleic acid. The lipoxygenase exhibited activity from pH 7 to 9 with optimum pH at 7.5. The enzyme was rapidly inactivated at temperatures above 40°C. Stability of gill lipoxygenase was enhanced in the presence of glutathione. Inactivation of lipoxygenase by sulfhydryl-specific reagents suggested that thiol groups were involved in its activity.",

author = "Hsieh, {Rudolf J.} and German, {J. Bruce} and Kinsella, {John E.}",

year = "1988",

language = "English (US)",

volume = "36",

pages = "680--685",

journal = "Journal of Agricultural and Food Chemistry",

issn = "0021-8561",

publisher = "American Chemical Society",

number = "4",

}

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T1 - Lipoxygenase in fish tissue

T2 - Some properties of the 12-lipoxygenase from trout gill

AU - Hsieh, Rudolf J.

AU - German, J. Bruce

AU - Kinsella, John E.

PY - 1988

Y1 - 1988

N2 - The gill and skin tissues from several fish species contain active lipoxygenase, which is capable of oxidizing polyunsaturated fatty acids into hydroperoxides. Gill lipoxygenase of rainbow trout exhibited similar reactivities toward arachidonic, eicosapentaenoic, and docosahexaenoic acids, but low reactivity toward linoleic acid. The lipoxygenase exhibited activity from pH 7 to 9 with optimum pH at 7.5. The enzyme was rapidly inactivated at temperatures above 40°C. Stability of gill lipoxygenase was enhanced in the presence of glutathione. Inactivation of lipoxygenase by sulfhydryl-specific reagents suggested that thiol groups were involved in its activity.

AB - The gill and skin tissues from several fish species contain active lipoxygenase, which is capable of oxidizing polyunsaturated fatty acids into hydroperoxides. Gill lipoxygenase of rainbow trout exhibited similar reactivities toward arachidonic, eicosapentaenoic, and docosahexaenoic acids, but low reactivity toward linoleic acid. The lipoxygenase exhibited activity from pH 7 to 9 with optimum pH at 7.5. The enzyme was rapidly inactivated at temperatures above 40°C. Stability of gill lipoxygenase was enhanced in the presence of glutathione. Inactivation of lipoxygenase by sulfhydryl-specific reagents suggested that thiol groups were involved in its activity.

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JO - Journal of Agricultural and Food Chemistry

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