Identification and characterization of a 15-lipoxygenase from fish gills

J. Bruce German, Richard K. Creveling

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

An arachidonic acid 15-lipoxygenase activity was discovered in the gill tissue of teleost fishes during purification of the previously recognized and more preponderant 12-lipoxygenase enzyme. The total activity of this enzyme following purification using hydroxylapatite was significantly greater than in the crude tissue preparation, suggesting that an inhibition was removed during purification. The enzyme was active toward polyunsaturated fatty acids present in the tissue producing hydroxylated metabolites from fatty acids with 18-, 20-, and 22-carbon chain lengths at carbons 13, 15, and 17, respectively The enzyme was further purified by using a Superose gel filtration column and eluted with an apparent molecular weight of 70 000.

Original languageEnglish (US)
Pages (from-to)2144-2147
Number of pages4
JournalJournal of Agricultural and Food Chemistry
Volume38
Issue number12
StatePublished - 1990

Fingerprint

Arachidonate 15-Lipoxygenase
lipoxygenase
Fish
gills
Fishes
Purification
Enzymes
Tissue
enzymes
fish
Carbon
carbon
Arachidonate 12-Lipoxygenase
arachidonic acid
polyunsaturated fatty acids
Durapatite
Metabolites
Unsaturated Fatty Acids
Chain length
gels

ASJC Scopus subject areas

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

Cite this

Identification and characterization of a 15-lipoxygenase from fish gills. / German, J. Bruce; Creveling, Richard K.

In: Journal of Agricultural and Food Chemistry, Vol. 38, No. 12, 1990, p. 2144-2147.

Research output: Contribution to journalArticle

German, J. Bruce ; Creveling, Richard K. / Identification and characterization of a 15-lipoxygenase from fish gills. In: Journal of Agricultural and Food Chemistry. 1990 ; Vol. 38, No. 12. pp. 2144-2147.
@article{ca172b2014f042e6a906b3024e325e49,
title = "Identification and characterization of a 15-lipoxygenase from fish gills",
abstract = "An arachidonic acid 15-lipoxygenase activity was discovered in the gill tissue of teleost fishes during purification of the previously recognized and more preponderant 12-lipoxygenase enzyme. The total activity of this enzyme following purification using hydroxylapatite was significantly greater than in the crude tissue preparation, suggesting that an inhibition was removed during purification. The enzyme was active toward polyunsaturated fatty acids present in the tissue producing hydroxylated metabolites from fatty acids with 18-, 20-, and 22-carbon chain lengths at carbons 13, 15, and 17, respectively The enzyme was further purified by using a Superose gel filtration column and eluted with an apparent molecular weight of 70 000.",
author = "German, {J. Bruce} and Creveling, {Richard K.}",
year = "1990",
language = "English (US)",
volume = "38",
pages = "2144--2147",
journal = "Journal of Agricultural and Food Chemistry",
issn = "0021-8561",
publisher = "American Chemical Society",
number = "12",

}

TY - JOUR

T1 - Identification and characterization of a 15-lipoxygenase from fish gills

AU - German, J. Bruce

AU - Creveling, Richard K.

PY - 1990

Y1 - 1990

N2 - An arachidonic acid 15-lipoxygenase activity was discovered in the gill tissue of teleost fishes during purification of the previously recognized and more preponderant 12-lipoxygenase enzyme. The total activity of this enzyme following purification using hydroxylapatite was significantly greater than in the crude tissue preparation, suggesting that an inhibition was removed during purification. The enzyme was active toward polyunsaturated fatty acids present in the tissue producing hydroxylated metabolites from fatty acids with 18-, 20-, and 22-carbon chain lengths at carbons 13, 15, and 17, respectively The enzyme was further purified by using a Superose gel filtration column and eluted with an apparent molecular weight of 70 000.

AB - An arachidonic acid 15-lipoxygenase activity was discovered in the gill tissue of teleost fishes during purification of the previously recognized and more preponderant 12-lipoxygenase enzyme. The total activity of this enzyme following purification using hydroxylapatite was significantly greater than in the crude tissue preparation, suggesting that an inhibition was removed during purification. The enzyme was active toward polyunsaturated fatty acids present in the tissue producing hydroxylated metabolites from fatty acids with 18-, 20-, and 22-carbon chain lengths at carbons 13, 15, and 17, respectively The enzyme was further purified by using a Superose gel filtration column and eluted with an apparent molecular weight of 70 000.

UR - http://www.scopus.com/inward/record.url?scp=0038949027&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0038949027&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:0038949027

VL - 38

SP - 2144

EP - 2147

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

SN - 0021-8561

IS - 12

ER -