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The alkylating agent 2-bromo-4'-nitroacetophenone (BrNAP) binds covalently to each of 10 isozymes of purified rat liver microsomal cytochrome P-450 (P-450a-P-450j) but substantially inhibits the catalytic activity of only cytochrome P-450c. Regardless of pH, incubation time, presence of detergents, or concentration of BrNAP, treatment of cytochrome P-450c with BrNAP resulted in no more than 90 ...
BrNAP-2 were identical (see footnote to Table 111) and that In summary, the results of the present study show that they corresponded to peptide T-36 previously sequenced from BrNAP alkylates each of 10 purified isozymes of rat liver unalkylatedcytochrome P-45Oc (18). Theamino acid se- microsomal cytochromeP-450 (P-450a-P-450j), as well as 11486 ...
The alkylating agent 2-bromo-4'-nitroacetophenone (BrNAP) binds covalently to each of 10 isozymes of purified rat liver microsomal cytochrome P-450 (P-450a-P-450j) but substantially inhibits the catalytic activity of only cytochrome P-450c. Regardless of pH, incubation time, presence of detergents, or concentration of BrNAP, treatment of ...
The mechanism by which 2-bromo-4'-nitroacetophenone (BrNAP) inactivates cytochrome P-450c, which involves alkylation primarily at Cys-292, is shown in the present study to involve an uncoupling of NADPH utilization and oxygen consumption from product formation. Alkylation of cytochrome P-450c with BrNAP markedly stimulated (approximately 30-fold) its rate of anaerobic reduction by NADPH ...
The alkylating agent 2-bromo-4'-nitroacetophenone (BrNAP) binds covalently to each of 10 isozymes of purified rat liver microsomal cytochrome P-450 (P-450a-P-450j) but substantially inhibits the catalytic activity of only cytochrome P-450c. Regardless of pH, incubation time, presence of detergents, or concentration
Objective Bacterial RNA polymerase (bRNAP) represent a crucial target for curtailing microbial activity but its structural and sequence similarities with human RNA polymerase II (hRNAPII) makes it difficult to target. Recently, Pseudouridimycin (PUM), a novel nucleoside analogue was reported to selectively inhibit bRNAP and not hRNAP. Till date, underlying mechanisms of PUM selectivity remains ...
The mechanism by which 2-bromo-4'-nitroacetophenone (BrNAP) inactivates cytochrome P-450c, which involves alkylation primarily at Cys-292, is shown in the present study to involve an uncoupling of ...
Objective: Bacterial RNA polymerase (bRNAP) represent a crucial target for curtailing microbial activity but its structural and sequence similarities with human RNA polymerase II (hRNAPII) makes it difficult to target. Recently, Pseudouridimycin (PUM), a novel nucleoside analogue was reported to selectively inhibit bRNAP and not hRNAP. Till date, underlying mechanisms of PUM selectivity ...
The independently determined yRNAP and bRNAP structures reveal that five 'core' subunits underlie a general RNAP architecture. The two large subunits form the central mass of the enzyme and opposite sides of a positively charged cleft (Rpb1 and Rpb2 in yRNAP; β′ and β in bRNAP; Table 1, Fig. 1).The two large subunits are anchored by two small core subunits that are involved in RNAP ...
Brná (German: Birnai), also known as Brná nad Labem to distinguish from other places with the same name, is an administrative part and residential area in Ústí nad Labem, Czech Republic.It is located in landscape park České Středohoří on the right side of river Elbe.It is about 4 km far from Ústí nad Labem and its area is about 4.23 km². [2]