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    Eur J Biochem. 1991 Dec 18;202(3):1231-8.

    Purification of two forms of arachidonate 15-lipoxygenase from human leukocytes.

    Izumi T, Rådmark O, Jörnvall H, Samuelsson B.

    Department of Physiological Chemistry, Karolinska Institutet, Stockholm, Sweden.

    Two different proteins with arachidonate 15-lipoxygenase activity have been purified to near homogeneity from human leukocytes. Both have the same molecular mass (74 kDa) on SDS/PAGE and appear to be equally active with three different fatty acid substrates. The N-terminal amino acid sequences of both forms were identical to the sequence of human reticulocyte 15-lipoxygenase [Sigal, E., Craik, C.S., Highland, E., Grunberger, D., Costello, L.L., Dixon, R.A.F. & Nadel, J.A. (1988) Biochem. Biophys. Res. Commun. 157, 457-464]. The two forms of 15-lipoxygenase could be clearly separated by cation-exchange chromatography. Of particular interest, the relative amounts of the two forms differed markedly between leukocytes obtained from normal donors and leukocytes from an individual with eosinophilia.

    PMID: 1662607 [PubMed - indexed for MEDLINE]

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