TY - JOUR
T1 - Cloning and sequence analysis of the cDNA for arachidonate 12-lipoxygenase of porcine leukocytes
AU - Yoshimoto, T.
AU - Suzuki, H.
AU - Yamamoto, S.
AU - Takai, T.
AU - Yokoyama, C.
AU - Tanabe, T.
PY - 1990
Y1 - 1990
N2 - The complete amino acid sequence of arachidonate 12-lipoxygenase (EC 1.13.11.31) of porcine leukocytes was deduced by cloning and sequence analysis of DNA complementary to its mRNA. The sequence was confirmed by automated Edman degradation of the N-terminal regions of the native enzyme and its proteolytic fragments. The cDNA had an open reading frame encoding 662 amino acid residues with a calculated molecular weight of 74,911. Amino acid residues 533-545, Cys-(Xaa)3-Cys-(Xaa)3-His-(Xaa)3-His, showed significant homology to the short cysteine- or histidine-containing sequences proposed as he metal-binding domains of transcription factors and various metal-containing proteins [Berg, J.M. (1986) Science 232, 485-487]. The amino acid sequence of 12-lipoxygenase exhibited 86% identity with human reticulocyte 15-lipoxygenase and showed 41% identity with human leukocyte 5-lipoxygenase. The 12-lipoxygenase cDNA recognized a 3.4-kilobase mRNA species in various porcine cell types, with the largest amount in leukocytes, followed by pituitary, lung, jejunum, and spleen.
AB - The complete amino acid sequence of arachidonate 12-lipoxygenase (EC 1.13.11.31) of porcine leukocytes was deduced by cloning and sequence analysis of DNA complementary to its mRNA. The sequence was confirmed by automated Edman degradation of the N-terminal regions of the native enzyme and its proteolytic fragments. The cDNA had an open reading frame encoding 662 amino acid residues with a calculated molecular weight of 74,911. Amino acid residues 533-545, Cys-(Xaa)3-Cys-(Xaa)3-His-(Xaa)3-His, showed significant homology to the short cysteine- or histidine-containing sequences proposed as he metal-binding domains of transcription factors and various metal-containing proteins [Berg, J.M. (1986) Science 232, 485-487]. The amino acid sequence of 12-lipoxygenase exhibited 86% identity with human reticulocyte 15-lipoxygenase and showed 41% identity with human leukocyte 5-lipoxygenase. The 12-lipoxygenase cDNA recognized a 3.4-kilobase mRNA species in various porcine cell types, with the largest amount in leukocytes, followed by pituitary, lung, jejunum, and spleen.
KW - 15-lipoxygenase
KW - 5-lipoxygenase
KW - arachidonic acid
KW - iron-binding domain
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U2 - 10.1073/pnas.87.6.2142
DO - 10.1073/pnas.87.6.2142
M3 - Article
C2 - 2315307
AN - SCOPUS:0025239471
SN - 0027-8424
VL - 87
SP - 2142
EP - 2146
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 6
ER -