English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  A spin-label electron spin resonance study of the binding of mitochondrial creatine kinase to cardiolipin.

Cheneval, D., Carafoli, E., Powell, G. L., & Marsh, D. (1989). A spin-label electron spin resonance study of the binding of mitochondrial creatine kinase to cardiolipin. European Journal of Biochemistry, 186(1-2), 416-419. doi:10.1111/j.1432-1033.1989.tb15225.x.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-B8BD-9 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-B8BE-7
Genre: Journal Article

Files

show Files
hide Files
:
2358983.pdf (Publisher version), 411KB
Name:
2358983.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Cheneval, D., Author
Carafoli, E., Author
Powell, G. L., Author
Marsh, D.1, Author              
Affiliations:
1Department of Spectroscopy and Photochemical Kinetics, MPI for biophysical chemistry, Max Planck Society, ou_578624              

Content

show
hide
Free keywords: -
 Abstract: The binding of the mitochondrial creatine kinase to aqueous dispersions of beef heart cardiolipin has been studied via the perturbation of the mobility of spin-labelled cardiolipin, using electron spin resonance (ESR) spectroscopy. In the presence of creatine kinase (1:1 protein/lipid ratio, by mass), the ESR spectra of cardiolipin labelled in a single acyl chain [n-(4,4-dimethyl-oxazolidinyl-N-oxy)stearoylcardiolipin] indicate a restriction of motion both at the C-5 and C-14 positions (n = 5, 14) of the lipid chains. The restriction in mobility was reversed by addition of phosphate or adriamycin, which are thought to inhibit the binding of creatine kinase to the rnitochondrial membrane or to displace it from its binding site on the membrane. The effect of the protein on the chain mobility is consistent with surface binding of the protein; no positive evidence was obtained for penetration of the protein into the hydrophobic region of the membrane.

Details

show
hide
Language(s): eng - English
 Dates: 1989-12
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: European Journal of Biochemistry
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 186 (1-2) Sequence Number: - Start / End Page: 416 - 419 Identifier: -