Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Characterization of the binding of benzo(a)pyrene (BP) to a 4S cytosolic protein

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:5325417
The authors have recently reported on the partial purification of a 4S binding protein that interacts in a specific and saturable manner with (/sup 3/H)BP and other polycyclic aromatic hydrocarbons (PAH). They also reported that the 4S binding protein was able to interact in a specific and saturable manner with plasmids collectively containing the rat cytochrome P450c gene. The authors have examined further the (/sup 3/H)BP binding properties of the 4S protein. The specific (/sup 3/H)BP binding activity appears to be highest in 4 week old male rats and declines with age. In some animals the specific (/sup 3/H)BP binding activity is induced after pretreatment with either phenobarbital (BP) or isosafrole (IS) as evidenced by a 75% and 52% increase, respectively, over untreated controls. No apparent increase was observed after pretreatment of animals with 3-methylcholanthracene (3MC). The addition of a 200 fold excess of tetra-chlordibenzofuran (TCDBF) to the incubations did not displace (/sup 3/H)BP from the 4S protein. The addition of molybdate (10 mM) to isolation buffers, known to stabilize certain hormone receptors, did not alter the sedimentation coefficient or the specific binding activity of the 4S protein. The authors conclude that: (1) in the rat, the 4S protein appears to be distinct from the 8S protein reported in the mouse and that: (2) the 4S species regulates the PAH induced expression of AHH activity in the rat.
Research Organization:
Univ. of Nebraska Medical Center, Omaha
OSTI ID:
5325417
Report Number(s):
CONF-8604222-
Conference Information:
Journal Name: Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States) Journal Volume: 45:3
Country of Publication:
United States
Language:
English