Identification of the Main Human Cytochrome P450 Enzymes Involved in Safrole 1'-Hydroxylation (Record no. 52894)

MARC details
000 -LEADER
fixed length control field 02192nam a2200217Ia 4500
003 - CONTROL NUMBER IDENTIFIER
control field MX-MdCICY
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20250625162418.0
040 ## - CATALOGING SOURCE
Transcribing agency CICY
090 ## - LOCALLY ASSIGNED LC-TYPE CALL NUMBER (OCLC); LOCAL CALL NUMBER (RLIN)
Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) B-18748
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION
fixed length control field 250602s9999 xx |||||s2 |||| ||und|d
245 10 - TITLE STATEMENT
Title Identification of the Main Human Cytochrome P450 Enzymes Involved in Safrole 1'-Hydroxylation
490 0# - SERIES STATEMENT
Volume/sequential designation Chem. Res. Toxicol., p.1151-1156, 2004
520 3# - SUMMARY, ETC.
Summary, etc. Safrole is a natural plant constituent, found in sassafras oil and certain other essential oils. The carcinogenicity of safrole is mediated through 1'-hydroxysafrole formation, followed by sulfonation to an unstable sulfate that reacts to form DNA adducts. To identify the main cytochrome P450 (P450)involved in human hepatic safrole 1'-hydroxylation (SOH), we determined the SOH activities of human liver microsomes andEscherichia colimembranes expressing bicistronic human P450s. Human liver (n)18)microsomal SOH activities were in the range of 3.5-16.9 nmol/min/mg protein with a mean value of 8.7(0.7 nmol/min/mg protein. In human liver (n)3)microsomes, the meanKmandVmaxvalues of SOH were 5.7(1.2 mM and 0.14(0.03µmol/min/nmol P450, respectively. The mean intrinsic clearance (Vmax/Km)was 25.3(2.3µL/min/nmol P450. SOH was sensitive to the inhibition by a CYP2C9 inhibitor, sulfaphenazole, and CYP2E1 inhibitors, 4-methylpyrazole and diethyldithiocarbamate. The liver microsomal SOH activity showed significant correlations with tolbutamide hydroxylation (r )0.569)and chlorzoxazone hydroxylation (r )0.770)activities, which were the model reactions catalyzed by CYP2C9 and CYP2E1, respectively. Human CYP2C9 and CYP2E1 showed SOH activities at least 2-fold higher than the other P450s. CYP2E1 showed an intrinsic clearance 3-fold greater than CYP2C9. These results demonstrated that CYP2C9 and CYP2E1 were the main P450s involved in human hepatic SOH.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Ueng, Yune-Fang
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Hsieh, Chih-Hang
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Don, Ming-Jaw
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Chi, Chin-Wen
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Ho, Li-Kang
856 40 - ELECTRONIC LOCATION AND ACCESS
Uniform Resource Identifier <a href="https://drive.google.com/file/d/1haFdDQ2z7NqBRWSueJ30BMd-NR-Mbf_b/view?usp=drivesdk">https://drive.google.com/file/d/1haFdDQ2z7NqBRWSueJ30BMd-NR-Mbf_b/view?usp=drivesdk</a>
Public note Para ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
942 ## - ADDED ENTRY ELEMENTS (KOHA)
Source of classification or shelving scheme Clasificación local
Koha item type Documentos solicitados
Holdings
Lost status Source of classification or shelving scheme Damaged status Not for loan Collection Home library Current library Shelving location Date acquired Total checkouts Full call number Date last seen Price effective from Koha item type
  Clasificación local     Ref1 CICY CICY Documento préstamo interbibliotecario 25.06.2025   B-18748 25.06.2025 25.06.2025 Documentos solicitados