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Published on: December 23, 2010
Purification of human leukotriene C4 synthase
J F Penrose1, L Gagnon, M Goppelt-Struebe
1Department of Rheumatology and Immunology, Brigham and Women's Hospital, Boston, MA.
Summary
Leukotriene C4 synthase was purified to homogeneity from myeloid cells. The enzyme was identified as an 18 kDa protein, consistent with its role in the microsomal glutathione S-transferase family.
Area of Science:
- Biochemistry
- Enzymology
- Molecular Biology
Background:
- Leukotriene C4 (LTC4) synthase catalyzes a key step in leukotriene biosynthesis.
- Understanding LTC4 synthase is crucial for inflammatory and allergic disease research.
Purpose of the Study:
- To purify and characterize Leukotriene C4 (LTC4) synthase.
- To determine the molecular weight of LTC4 synthase.
Main Methods:
- Microsomal solubilization using sodium deoxycholate and Triton X-102.
- Affinity chromatography with S-hexyl-glutathione-agarose.
- Nondenaturing and SDS-PAGE electrophoresis with silver staining.
Main Results:
- LTC4 synthase was purified to homogeneity from KG-1 myeloid cells.
- A single protein band of 18 kDa was consistently associated with LTC4 synthase activity.
- The purified enzyme exhibited 12.5% overall recovery.
Conclusions:
- Leukotriene C4 (LTC4) synthase is identified as an 18 kDa protein.
- The 18 kDa size is consistent with LTC4 synthase belonging to the microsomal glutathione S-transferase family.
