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J. Biol. Chem., Vol. 263, Issue 8, 3550-3553, Mar, 1988
JP Merlie, D Fagan, J Mudd and P Needleman
An oligonucleotide probe was used to isolate a clone encoding prostaglandin
endoperoxide synthetase (cyclooxygenase, EC 1.14.99.1) from a sheep seminal
vesicle cDNA library. The protein predicted from nucleic acid sequence
contains 599 amino acids including a 23-amino acid signal sequence. Thus,
the mature cyclooxygenase deduced from the cDNA compares favorably in
molecular size to the 70-kDa protein determined by gel electrophoresis. A
putative transmembrane region and potential carbohydrate addition sites for
N-linked sugars can be inferred from the amino acid sequence.
Significantly, sequence similarities exist between cyclooxygenase,
myeloperoxidase, and several other heme-containing proteins. The putative
glycosylation sites, transmembrane domain, and sequence similarities with
functionally related enzymes have been incorporated into a model for the
topology of cyclooxygenase in the endoplasmic reticulum.
Isolation and characterization of the complementary DNA for sheep seminal vesicle prostaglandin endoperoxide synthase (cyclooxygenase)
Department of Pharmacology, Washington University School of Medicine, St. Louis, Missouri 63110.
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