In:
European Journal of Biochemistry, Wiley, Vol. 202, No. 3 ( 1991-12), p. 1231-1238
Abstract:
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.
Type of Medium:
Online Resource
ISSN:
0014-2956
,
1432-1033
DOI:
10.1111/ejb.1991.202.issue-3
DOI:
10.1111/j.1432-1033.1991.tb16495.x
Language:
English
Publisher:
Wiley
Publication Date:
1991
detail.hit.zdb_id:
1398347-7
detail.hit.zdb_id:
2172518-4
SSG:
12
Bookmarklink