Molecular cloning of human platelet thromboxane A synthase.
Article Details
- CitationCopy to clipboard
Yokoyama C, Miyata A, Ihara H, Ullrich V, Tanabe T
Molecular cloning of human platelet thromboxane A synthase.
Biochem Biophys Res Commun. 1991 Aug 15;178(3):1479-84.
- PubMed ID
- 1714723 [ View in PubMed]
- Abstract
Complementary DNA coding for thromboxane A synthase was amplified by polymerase chain reaction using primers synthesized according to the partial amino acid sequences of human platelet thromboxane A synthase (Nusing, R., Schneider-Voss, S., and Ullrich, V. (1990) Arch. Biochem. Biophys. 280, 325-330) and cloned into pBluescript SK II(-). The primary structure of human platelet enzyme was deduced from the nucleotide sequence of the cDNA. The enzyme is composed of 533 amino acids with a molecular weight of 60,487. The primary structure of the enzyme exhibited a 34-36% homology to the amino acid sequences of cytochrome P450s classified in the P450 III gene family. The highly conserved cysteine-containing sequence involved in the heme-binding site of P450 was found near the carboxyl terminus (residues 472-492). The size of the major thromboxane A synthase mRNA from human platelets and human erythroleukemia cells was estimated to be approximately 2.2 kilobases by RNA blot analysis.