Primary structure of the cholesterol side-chain cleavage cytochrome P-450 from bovine adrenocortical mitochondria and some aspects of its functioning on a structural level

Chashchin, Vadim L.; Lapko, Veniamin N.; Adamovich, T.B.; Лапко, А. Г.; Kuprina, N.S.; Ахрем, А. А.

doi:10.1016/0167-4838(86)90176-7

Cited by 15 publications

(3 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The pellet was resuspended in 1 ml buffer and the supernatant was concentrated to the same volume for SDS-PAGE samples preparation [4]. Trypsinolysis of purified P-450scc and separation of F~, F2 and F3 were carried out as described in [2]. P-450scc concentration was determined as in [7].…”

Section: Purification and Proteolysis Proceduresmentioning

confidence: 99%

See 1 more Smart Citation

Inhibitory domain‐specific antibodies to cytochrome P‐450_scc

Usanov¹,

Chernogolov²,

Chashchin³

1989

FEBS Letters

View full text Add to dashboard Cite

Highly specific antibodies to cytochrome P-450~ and its F~ and F 2 fragments, representing N-and C-terminal sequences of the hemeprotein respectively, were raised in rabbits. These antibodies were found to be inhibitory (up to 50-90%) for the cholesterol transformation into pregnenolone in the reconstituted system, indicating the involvement of both F 1 and F 2 domains formed by the respective fragments in monooxygenase catalysis. Cytoehrome P-450~¢ in mitoplasts is not accessible for trypsin as revealed by immunological techniques. However, the treatment of submitochondrial particles with trypsin results in two main fragments identified by immunoblotting in the presence of the monospecific antibodies as F~ and F 2 fragments. This indicates that the trypsin sensitive 250-257 region in cytochrome P-450~ molecule connecting both domains is exposed to the matrix side of the inner mitochondrial membrane.

show abstract

Section: Purification and Proteolysis Proceduresmentioning

confidence: 99%

“…Limited proteolysis of the native purified P-450~¢¢ with trypsin results in two large fragments: F1 with molecular weight of 29 800 Da and F2 of 26 600 Da [2], corresponding to N-and C-terminal sequences of the hemeprotein, respectively ( fig. 1).…”

Section: Introductionmentioning

confidence: 99%

Inhibitory domain‐specific antibodies to cytochrome P‐450_scc

Usanov¹,

Chernogolov²,

Chashchin³

1989

FEBS Letters

View full text Add to dashboard Cite

show abstract

“…В нашей работе мы использовали митохондриальный ген из коры надпочечников быка сур11А1, кодирующий цитохром Р450scc. Цитохром P450scc является ключевым ферментом стероидогенеза в тканях животных, отщепляет боковую цепь холестерола и превращает его в прегнено-лон [8,20,21,24,27]. Основные стадии метаболизма стероидных гормонов животных и брассиностероидов растений сходны [7,10,12,17,19,22].…”

unclassified

BIOMETRIC ANALYSIS OF TRANSGENIC PLANTS OF SPRING RAPE WITH cyp11A1 ANIMAL ORIGIN GENE AND BACTERIAL bar

Shishlova-Sokolovskaya¹,

Kartel²,

Shishlov³

et al. 2017

Fiziol. rast. genet.

View full text Add to dashboard Cite

В результате Agrobacterium-опосредованной трансформации рапса получены трансгенные растения, несущие в геноме гены сур11А1 и bar. Растения характеризовались увеличением длины главной кисти, массы 1000 семян, количества стручков и боковых побегов главной кисти в семенных поколениях по сравнению с контрольными. При этом признаки массы 1000 семян и высота растений оказались наименее изменчивыми.Ключевые слова: Brassica napus L. var. oleifera DC., трансгенные растения, биометрический анализ, ген сур11А1, ген bar.

show abstract