Isolation of partial complementary DNA encoding human thromboxane synthase.
Thromboxane synthase catalyzes the biosynthesis of thromboxane A2 which plays a key role in the proaggregatory and vasoconstrictive processes. In this communication, we reported the successful cloning of thromboxane synthase cDNA from a human lung cDNA library. Oligonucleotides were synthesized according to the direct amino acid sequence of 2 peptides derived from purified human thromboxane synthase. Polymerase chain reaction was carried out using these oligonucleotides as primers to isolate a complementary DNA from human lung cDNA library. The longest cDNA thus obtained was 687 base pairs in length. Amino acid sequences deduced from the cDNA contained all three peptide sequences reported, confirming the authenticity of the cDNA clone.
Wang
L H
LH
Department of Internal Medicine, University of Texas Medical School, Houston 77030.
Ohashi
K
K
Wu
K K
KK
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics* / Q000302:isolation & purification; D015723:Gene Library; D006801:Humans; D008168:Lung / Q000201:enzymology; D008969:Molecular Sequence Data; D015345:Oligonucleotide Probes; D016133:Polymerase Chain Reaction / Q000379:methods; D013930:Thromboxane-A Synthase / Q000235:genetics*
D015345:Oligonucleotide Probes; D004247:DNA; D013930:Thromboxane-A Synthase