Purification of a Single Major Form of Microsomal Cytochrome P-450 from Tulip Bulbs (Tulipa gesneriana L.) |
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Authors: | Ken Higashi Kie Ikeuchi Masanobu Obara Yuji Karasaki Hideyasu Hirano Sadao Gotoh |
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Institution: | Department of Biochemistry, University of Occupational and Environmental Health, Kitakyushu 807, Japan |
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Abstract: | Microsomal cytochrome P-450 from tulip bulbs (Tulipa gesneriana L., Balalaika) was purified to an almost electrophoretically homogeneous preparation. The specific content of cytochrome P-450 in the final preparation was 6.68 nmol/mg protein, which was 30-fold enriched from that of the solubilized fractions of microsomes. The molecular weight of purified cytochrome P-450 by SDS-gel electrophoresis is 52,500. The Oxidized form of the purified cytochrome P-450 had absorption peaks at 392, 552, and 645 nm and the absolute reduced CO spectrum peaked at 448 nm. Judged spectrally, the purified cytochrome P-450 is in high spin in the oxidized state. Antiserum against this cytochrome P-450 previously has shown to be highly specific for its antigen but showed a single precipitin line with solubilized microsomal proteins from tulip bulbs of several other cultivars. The physiological role of this cytochrome P-450, however, is unknown in these dormant tulip bulbs. |
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