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Isolation and characterization of an altered cytochrome P-450 from a yeast mutant defective in lanosterol 14 alpha-demethylation.
Aoyama Y, Yoshida Y, Nishino T, Katsuki H, Maitra US, Mohan VP, Sprinson DB. Aoyama Y, et al. J Biol Chem. 1987 Oct 15;262(29):14260-4. J Biol Chem. 1987. PMID: 3115990 Free article.
A cytochrome P-450 (P-450SG1) was purified from a lanosterol 14 alpha-demethylase (P-450(14DM)) defective mutant of Saccharomyces cerevisiae, strain SG1, by a method similar to that used in the purification of the wild type enzyme (Yoshida, Y., and Aoyama, Y. …
A cytochrome P-450 (P-450SG1) was purified from a lanosterol 14 alpha-demethylase (P-450(14DM)) defective mutant of Saccharomyces cerevisiae …
Altered cytochrome P-450 in a yeast mutant blocked in demethylating C-32 of lanosterol.
Aoyama Y, Yoshida Y, Hata S, Nishino T, Katsuki H, Maitra US, Mohan VP, Sprinson DB. Aoyama Y, et al. J Biol Chem. 1983 Aug 10;258(15):9040-2. J Biol Chem. 1983. PMID: 6409899 Free article.
On the other hand, cholate-solubilized microsomes from SG1 formed a single precipitin line on Ouchterlony plates with antibodies raised against purified (Yoshida, Y., Aoyama, Y., Kumaoka, H., and Kubota, S. (1977) Biochem. Biophys. ...
On the other hand, cholate-solubilized microsomes from SG1 formed a single precipitin line on Ouchterlony plates with antibodies raised agai …
972 results