Isolation and characterization of the complementary DNA for sheep seminal vesicle prostaglandin endoperoxide synthase (cyclooxygenase).
作者： J P Merlie , D Fagan , J Mudd , P Needleman
DOI: 10.1016/S0021-9258(18)68959-8
关键词: Transmembrane domain 、 Molecular biology 、 Nucleic acid sequence 、 Peptide sequence 、 Gel electrophoresis 、 Biology 、 Biochemistry 、 Amino acid 、 Signal peptide 、 cDNA library 、 Complementary DNA
摘要: An oligonucleotide probe was used to isolate a clone encoding prostaglandin endoperoxide synthetase (cyclooxygenase, EC 1.14.99.1) from sheep seminal vesicle cDNA library. The protein predicted nucleic acid sequence contains 599 amino acids including 23-amino signal sequence. Thus, the mature cyclooxygenase deduced compares favorably in molecular size 70-kDa determined by gel electrophoresis. A putative transmembrane region and potential carbohydrate addition sites for N-linked sugars can be inferred Significantly, similarities exist between cyclooxygenase, myeloperoxidase, several other heme-containing proteins. glycosylation sites, domain, with functionally related enzymes have been incorporated into model topology of endoplasmic reticulum.
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