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Related Experiment Videos

Isolation of partial complementary DNA encoding human thromboxane synthase.

L H Wang1, K Ohashi, K K Wu

  • 1Department of Internal Medicine, University of Texas Medical School, Houston 77030.

Biochemical and Biophysical Research Communications
|May 31, 1991
PubMed
Summary

Researchers successfully cloned thromboxane synthase cDNA from human lung tissue. This advancement aids in understanding thromboxane A2

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Enzymology

Background:

  • Thromboxane synthase is crucial for synthesizing thromboxane A2.
  • Thromboxane A2 significantly influences blood aggregation and blood vessel constriction.

Purpose of the Study:

  • To report the successful cloning of human thromboxane synthase cDNA.
  • To confirm the authenticity of the cloned cDNA sequence.

Main Methods:

  • Synthesized oligonucleotides based on purified human thromboxane synthase peptide sequences.
  • Employed polymerase chain reaction (PCR) with these oligonucleotides as primers.
  • Screened a human lung cDNA library to isolate the target complementary DNA (cDNA).

Main Results:

Related Experiment Videos

  • Successfully isolated a cDNA clone of thromboxane synthase.
  • The longest cDNA obtained measured 687 base pairs.
  • Deduced amino acid sequences from the cDNA matched the known peptide sequences, validating the clone.
  • Conclusions:

    • The successful cloning of human thromboxane synthase cDNA was achieved.
    • This molecular tool facilitates further research into thromboxane synthase function and regulation.