## Abstract In this study, CYP2B‐immunoreactive protein was purified to electrophoretic homogeneity from the liver microsomes of leaping mullet. The purified cytochrome P450 (CYP) gave a single band on sodium dodecyl sulfate–polyacrylamide gel electrophoresis having a __M__~r~ of 49,300 Da. Absolut
Further immunochemical and biocatalytic characterization of CYP1A1 from feral leaping mullet liver (Liza saliens) microsomes
✍ Scribed by Alaattin Şen; Emel Arinç
- Book ID
- 117567251
- Publisher
- Elsevier Science
- Year
- 2000
- Tongue
- English
- Weight
- 197 KB
- Volume
- 126
- Category
- Article
- ISSN
- 0742-8413
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NADPH-cytochrome P450 reductase was purified to electrophoretic homogeneity from detergent-solubilized liver microsomes from the leaping mullet (Liza saliens). The purified reductase was characterized with respect to spectral, electrophoretic, and biocatalytic properties. In addition, effects of pH,
## Abstract A 2,037 bp CYP1A1 cDNA (GenBank AF072899) was cloned through screening of a λZipLox cDNA library constructed from the liver of a leaping mullet (__Liza saliens__) fish captured from Izmir Bay on the Aegean coast of Turkey using rainbow trout CYP1A1 cDNA as a probe. This clone has a 130