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Publication : Cloning and characterization of a murine macrophage lipoxygenase.

First Author  Freire-Moar J Year  1995
Journal  Biochim Biophys Acta Volume  1254
Issue  1 Pages  112-6
PubMed ID  7811740 Mgi Jnum  J:22314
Mgi Id  MGI:70194 Doi  10.1016/0005-2760(94)00199-9
Citation  Freire-Moar J, et al. (1995) Cloning and characterization of a murine macrophage lipoxygenase. Biochim Biophys Acta 1254(1):112-6
abstractText  We have isolated a murine macrophage cDNA encoding a 12-lipoxygenase, that represents the homolog of the human 15-lipoxygenase. The predicted amino acid sequence of this lipoxygenase is highly similar to the rat 12-lipoxygenase isolated from brain and human 15-lipoxgenase. The recombinant enzyme expressed in Cos-7 cells oxidizes arachidonic acid to 12- and 15-HETE with a profile similar to that obtained from peritoneal macrophages. A polyclonal antibody generated against a putative peptide recognizes a 75 kDa protein in cell extracts from mouse peritoneal macrophages and transfected Cos-7 cells. The lipoxygenase cDNA hybridizes to a 2.5 kb mRNA present in peritoneal macrophages, lung, spleen, heart and liver. RT-PCR analysis indicates that the same lipoxygenase is expressed in mouse reticulocytes. A partial genomic clone for this lipoxygenase has also been characterized. Southern blot analysis of mouse genomic DNA indicates that this is a single copy gene.
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