U.S. flag An official website of the United States government.
Official websites use .gov

A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS

A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

i

Specificity in the Interaction of Phospholipids and Fatty Acids with Vesicle Reconstituted Cytochrome P-450: A Spin Label Study



Details

  • Personal Author:
  • Description:
    The association of fatty acids, androstane, phosphatidylcholine, phosphatidylethanolamine, and phosphatidic acid with purified and phospholipid-vesicle reconstituted cytochrome P-450was studied by spin labeling. Spin-labeled fatty acids were found to be motionally restricted by cytochrome P-450 in both phospholipid vesicles and in microsomes to a much greater extent than spin-labeled phospholipids. The equilibrium of spin-labeled fatty acid between the bulk membrane lipid and the protein interface could be shifted towards an increased amount in the bulk phospholipid phase by the addition of oleic acid or lysophosphatidylcholine, but not by sodium cholate. Microsomes from different animals showed a variable extent of motional restriction of fatty acids, independent of pretreatment of the animals with phenobarbital or beta-naphthoflavone, of cytochrome P-450 content, of the presence of type I and type II substrates for cytochrome P-450. These differences are attributed to the presence of varying amounts of lipid breakdown products in the microsomal membrane such as lysolipids or fatty acids which compete with the externally added spin-labeled fatty acids, or with spin-labeled androstane for the binding to cytochrome P-450. The negative charge of the fatty acid was found to be involved in its association with the protein. Cytochrome P-450 was shown to interact only with a few spin-labeled phospholipid molecules in such a way that the motional restriction of the spin acyl chains can be detected by electron paramagnetic resonance (TR>10^-8s). The number of associated lipid molecules per protein probably is too small to form a complete shell around the protein. This lipid-protein interaction could be destroyed by the addition of sodium cholate, in contrast to the fatty acid-protein interaction. [Description provided by NIOSH]
  • Subjects:
  • Keywords:
  • ISSN:
    0006-3002
  • Document Type:
  • Funding:
  • Genre:
  • Place as Subject:
  • CIO:
  • Topic:
  • Location:
  • Pages in Document:
    258-266
  • Volume:
    729
  • Issue:
    2
  • NIOSHTIC Number:
    nn:20060779
  • Citation:
    Biochim Biophys Acta 1983 Apr; 729(2):258-266
  • Federal Fiscal Year:
    1983
  • Performing Organization:
    Stanford University, Stanford, California
  • Peer Reviewed:
    True
  • Start Date:
    19800901
  • Source Full Name:
    Biochimica et Biophysica Acta
  • End Date:
    19901130
  • Collection(s):
  • Main Document Checksum:
    urn:sha-512:9161c7c66b44cfc4e53acd23d6e67e290b5939a87de8fecba88fcd950105d399bace120ff93ecd9d80a9a27be935ecd9fd04bd6f06e284821ecbd069b2861021
  • Download URL:
  • File Type:
    Filetype[PDF - 717.81 KB ]
ON THIS PAGE

CDC STACKS serves as an archival repository of CDC-published products including scientific findings, journal articles, guidelines, recommendations, or other public health information authored or co-authored by CDC or funded partners.

As a repository, CDC STACKS retains documents in their original published format to ensure public access to scientific information.