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Primary structure of a lipoxygenase from barley grain as deduced from its cDNA sequence

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Author: Mechelen, J.R. van · Smits, M. · Douma, A.C. · Rouster, J. · Cameron-Mills, V. · Heidekamp, F. · Valk, B.E.
Type:article
Date:1995
Institution: Centraal Instituut voor Voedingsonderzoek TNO
Source:Biochimica et Biophysica Acta - Lipids and Lipid Metabolism, 2, 1254, 221-225
Identifier: 232921
doi: DOI:10.1016/0005-2760(94)00231-M
Keywords: Nutrition · Barley · CDNA cloning · Hordeum vulgare L. · Inverse PCR cloning · LOX · Plant lipoxygenase · Lipoxygenase · Barley · Dna sequence · Enzyme analysis · Phytochemistry · Priority journal · Protein analysis · Amino Acid Sequence · Base Sequence · DNA, Complementary · Hordeum · Lipoxygenase · Molecular Sequence Data · Polymerase Chain Reaction · Sequence Analysis

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.