Print Email Facebook Twitter Primary structure of a lipoxygenase from barley grain as deduced from its cDNA sequence Title Primary structure of a lipoxygenase from barley grain as deduced from its cDNA sequence Author van Mechelen, J.R. Smits, M. Douma, A.C. Rouster, J. Cameron-Mills, V. Heidekamp, F. Valk, B.E. Centraal Instituut voor Voedingsonderzoek TNO Publication year 1995 Abstract A full length cDNA sequence for a barley grain lipoxygenase was obtained. It includes a 5' untranslated region of 69 nucleotides, an open reading frame of 2586 nucleotides encoding a protein of 862 amino acid residues and a 3' untranslated region of 142 nucleotides. The molecular mass of the encoded polypeptide was calculated to be 96.392. Its amino acid sequence shows a high homology with that of other plant lipoxygenases identified to date. Subject NutritionBarleyCDNA cloningHordeum vulgare L.Inverse PCR cloningLOXPlant lipoxygenaseLipoxygenaseBarleyDna sequenceEnzyme analysisPhytochemistryPriority journalProtein analysisAmino Acid SequenceBase SequenceDNA, ComplementaryHordeumLipoxygenaseMolecular Sequence DataPolymerase Chain ReactionSequence Analysis To reference this document use: http://resolver.tudelft.nl/uuid:d40b0284-e368-4f86-9045-d9ea532b0fd9 DOI https://doi.org/10.1016/0005-2760(94)00231-m TNO identifier 232921 ISSN 0005-2760 Source Biochimica et Biophysica Acta - Lipids and Lipid Metabolism, 1254 (2), 221-225 Document type article Files To receive the publication files, please send an e-mail request to TNO Library.