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.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
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.
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| skos:exactMatch | |
| uniprot:name |
Eur. J. Biochem.
|
| uniprot:author |
Izumi T.,
Joernvall H.,
Raadmark O.,
Samuelsson B.
|
| uniprot:date |
1991
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| uniprot:pages |
1231-1238
|
| uniprot:title |
Purification of two forms of arachidonate 15-lipoxygenase from human leukocytes.
|
| uniprot:volume |
202
|
| dc-term:identifier |
doi:10.1111/j.1432-1033.1991.tb16495.x
|