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Reticulocyte lipoxygenase, ingensin, and ATP-dependent proteolysis
FEBS Letters
|May 26, 1986
Summary
Rabbit reticulocyte lipoxygenase, a 68 kDa protein, is inhibited by several compounds. While some inhibitors affect both lipoxygenase and ATP-dependent proteolysis, ingensin, a protease, may play a key role in proteolysis.
Area of Science:
- Biochemistry
- Molecular Biology
- Enzymology
Background:
- Rabbit reticulocyte lysate contains lipoxygenase, an enzyme with a molecular mass of 68 kDa and a pI of 5.97.
- Lipoxygenase activity is sensitive to inhibitors like NDGA, BW755C, ETYA, SHAM, and hemin, but unaffected by metal ions or nucleotides.
Purpose of the Study:
- To investigate the relationship between lipoxygenase activity and ATP-dependent proteolysis in rabbit reticulocytes.
- To identify the specific protease responsible for casein degradation in reticulocyte extracts.
Main Methods:
- Purification of lipoxygenase and a high-molecular-mass protease (ingensin) from rabbit reticulocyte lysate.
- Enzyme activity assays for both lipoxygenase and proteolysis.
- Inhibition studies using various compounds including NDGA, SHAM, and o-phenanthroline.
Main Results:
- Lipoxygenase was purified and characterized.
- Several inhibitors affected both lipoxygenase and ATP-dependent proteolysis, but with differing potencies.
- Ingensin, a protease, accounted for over 90% of casein-degrading activity and was inhibited by NDGA at concentrations similar to those affecting proteolysis.
Conclusions:
- Lipoxygenase is not essential for ATP-dependent proteolysis in rabbit reticulocytes.
- The high-molecular-mass protease, ingensin, is likely involved in the ATP-dependent proteolysis process.
