Cloning and sequence analysis of the cDNA for arachidonate 12-lipoxygenase of porcine leukocytes

T. Yoshimoto, H. Suzuki, S. Yamamoto, T. Takai, C. Yokoyama, T. Tanabe

研究成果: Article査読

124 被引用数 (Scopus)


The complete amino acid sequence of arachidonate 12-lipoxygenase (EC 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.

ジャーナルProceedings of the National Academy of Sciences of the United States of America
出版ステータスPublished - 1990

ASJC Scopus subject areas

  • 一般


「Cloning and sequence analysis of the cDNA for arachidonate 12-lipoxygenase of porcine leukocytes」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。