Primary structure of a lipoxygenase from barley gr...[Biochim Biophys Acta. 1995]

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1: Biochim Biophys Acta. 1995 Jan 20;1254(2):221-5. Links

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

van Mechelen JR, Smits M, Douma AC, Rouster J, Cameron-Mills V, Heidekamp F, Valk BE.

Center for Phytotechnology, RUL/TNO, Department Molecular Plant Biotechnology, Leiden, The Netherlands.

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.

PMID: 7827128 [PubMed - indexed for MEDLINE]

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

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