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김수언,김인수,Kim, Soo-Un,Kim, In-Soo,Anderson, John A. 생화학분자생물학회 1985 한국생화학회지 Vol.18 No.3
Claviceps, purpurea PRL 1980의 microsome에는 단백질 mg 당 40 pmole의 cytochrome P-450이 함유되어 있었다. 이 microsome으로부터 단백질 mg 당 420 pmole의 cytochrome P-450 및 387 pmole의 NADPH-cytochrome c reductase로 정제하였다. 부분 정제된 이 두 단백질로 재구성을 시도하였을 때 agroclavine hydroxylase 활성을 나타내지 않았으나 NADPH-cytochrome c reductase를 microsome에 첨가하였을 경우에는 그 활성이 80% 증가되었다. Claviceps sp. SD58의 microsome에 있는 agroclavine hydroxylase의 $V_{max}$와 $K_m$값은 agroclavine에 대하여 각각 3.3 pkat와 0.11 mM 이었다. 또 이 균으로부터 정제된 cytochrome P-450과 기질인 agroclavine의 복합체는 제2특성을 갖는 spectrum을 나타내었다. 또 위의 두 균주로 부터 분리한 cytochrome P-450이 이산화탄소와 결합할때 그 difference spectrum의 최대흡광은 449 nm 이었다. Microsomes of Claviceps purpurea PRL 1980 had a maximum concentration of cytochrome P-450 of 40 pmole per mg protein. Cytochrome P-450 and NADPH-cy-to chrome c reductase were purified from C. purpurea PRL 1980 microsomes to concentrations of 421 pmole per mg protein and 387 pmole per min per mg protein, respectively. Activity was not reconstituted from these fractions, but NADPH-cytochrome c reductase increased agroclavine hydroxylase activity of C. purpurea PRL 1980 microsomes. The activity was not stimulated by rat liver microsomal NADPH -cytochrome c reductase. Claviceps sp. SD58 microsomal agroclavine hydroxylase had $V_{max}$ of 3.3 pkat per mg and $K_m$ of 0.11 mM for agroclavine. Agroclavine bound to cytochrome P-450 from Claviceps sp. SD58 to give a type II spectrum. The absorbance maximum in the CO-reduced vs reduced difference spectrum of purified cytochrome P-450 from C. purpurea PRL 1980 and Claviceps sp. SD58 was at 449 nm.
Claviceps sp . 에서 Cytochrome P - 450 및 NADPH - Cytochrome c Reductase 정제 및 그 특성
김수언,김인수,John A . Anderson ( Soo Un Kim,In Soo Kim,John A . Anderson ) 생화학분자생물학회 1985 BMB Reports Vol.18 No.3
Microsomes of Claviceps purpurea PRL 1980 had a maximum concentration of cytochrome P-450 of 40 pmole per ㎎ protein. Cytochrome P-450 and NADPH-cytochrome c reductase were purified from C. purpurea PRL 1980 microsomes to concentrations of 421 pmole per ㎎ protein and 387 pmole per min per mg protein, respectively. Activity was not reconstituted from these fractions, but NADPH-cytochrome c reductase increased agroclavine hydroxylase activity of C. purpurea PRL 1980 microsomes. The activity was not stimulated by rat liver microsomal NADPH-cytochrome c reductase. Claviceps sp. SD58 microsomal agroclavine hydroxylase had V_(max) of 3.3 pkat per ㎎ and K_m of 0.11 mM for agroclavine. Agroclavine bound to cytochrome P-450 from Claviceps sp. SD58 to give a type II spectrum. The absorbance maximum in the CO-reduced vs reduced difference spectrum of purified cytochrome P-450 from C. purpurea PRL 1980 and Claviceps sp. SD58 was at 449 ㎚.