My NCBI | Sign In
RSS Settings
  • Search:

Display Settings:

Format

Send to:

Choose Destination

    Biochim Biophys Acta. 1994 Mar 3;1211(2):239-42.

    The primary structure of a lipoxygenase from the shoots of etiolated lentil seedlings derived from its cDNA.

    Hilbers MP, Rossi A, Finazzi-Agrò A, Veldink GA, Vliegenthart JF.

    Department of Experimental Medicine and Biochemical Sciences, University of Rome Tor Vergata, Italy.

    Screening of a cDNA library constructed from the shoots of etiolated lentil seedlings resulted in finding a 2778 bp cDNA sequence, containing an open reading frame coding for a lipoxygenase of 866 amino acid residues. This lipoxygenase appears to be a novel type of vegetative lipoxygenase, different from the seed lipoxygenases of other leguminosae (complete homology < or = 72%).

    PMID: 8117753 [PubMed - indexed for MEDLINE]

    Publication Types, MeSH Terms, Substances, Secondary Source ID

    Publication Types:

    MeSH Terms:

    Substances:

    Secondary Source ID:

    LinkOut - more resources

    Full Text Sources:

    Supplemental Content

    Click here to read

    Related articles

    All links from this record

    • Related Articles

      Calculated set of PubMed citations closely related to the selected article(s) retrieved using a word weight algorithm. Related articles are displayed in ranked order from most to least relevant, with the “linked from” citation displayed first.

    • Nucleotide

      Primary database (GenBank) nucleotide records reported in the current articles as well as Reference Sequences (RefSeqs) that include the articles as references.

    • Substance (MeSH Keyword)

      PubChem chemical substance (submitted) records that are classified under the same Medical Subject Headings (MeSH) controlled vocabulary as the current articles.

    • Taxonomy via GenBank

      Taxonomy records associated with the current articles through taxonomic information on related molecular database records (Nucleotide, Protein, Gene, SNP, Structure).

    • Protein

      Protein translation features of primary database (GenBank) nucleotide records reported in the current articles as well as Reference Sequences (RefSeqs) that include the articles as references.

    Recent activity