Open AccessPurification of two forms of arachidonate 15‐lipoxygenase from human leukocytes
Author(s) -
IZUMI Takashi,
RÅDMARK Olof,
JÖRNVALL Hans,
SAMUELSSON Bengt
Publication year - 1991
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1991.tb16495.x
Subject(s) - lipoxygenase , reticulocyte , molecular mass , biochemistry , arachidonic acid , chemistry , arachidonate 5 lipoxygenase , cytoplasm , microbiology and biotechnology , enzyme , biology , gene , messenger rna
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., Criak, 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 donors and leukocyltes from an individual with eosinophilia.