Search: WFRF:(Ahnström G)
> (1987-1989) >
Energy-linked nicot...
-
Persson, Bengt L.Department of Biochemistry, Arrhenius Laboratory, University of Stockholm
(author)
Energy-linked nicotinamide nucleotide transhydrogenase. Hydrodynamic properties and active form of purified and membrane-bound mitochondrial transhydrogenase from beef heart
- Article/chapterEnglish1987
Publisher, publication year, extent ...
-
Elsevier BV,1987
-
printrdacarrier
Numbers
-
LIBRIS-ID:oai:DiVA.org:lnu-1169
-
https://urn.kb.se/resolve?urn=urn:nbn:se:lnu:diva-1169URI
-
https://doi.org/10.1016/0003-9861(87)90500-5DOI
Supplementary language notes
-
Language:English
-
Summary in:English
Part of subdatabase
Classification
-
Subject category:ref swepub-contenttype
-
Subject category:art swepub-publicationtype
Notes
-
The mitochondrial nicotinamide nucleotide transhydrogenase from beef heart was investigated with respect to minimal assembly of the purified enzyme and of the enzyme in the mitochondrial inner membrane. Studies of the hydrodynamic properties of the purified enzyme in the presence of 0.3% Triton X-100 allowed determination of the Stokes radius, sedimentation constant, partial specific volume, frictional ratio, and molecular weight. Under these conditions transhydrogenase existed as an inactive monomer, suggesting that monomerization may be accompanied by inactivation. Radiation inactivation was used to determine the functional molecular size of purified detergent-dispersed transhydrogenase and transhydrogenase in beef heart submitochondrial particles. Under these conditions the catalytic activity of both the purified and the membrane-bound enzyme was found to be catalyzed by a dimeric form of the enzyme. These results suggest for the first time that the minimal functional assembly of detergent-dispersed as well as membrane-bound transhydrogenase is a dimer, which is not functionally associated with, for example, complex I or ATPase. In addition, the results are consistent with the possibility that the two subunits of transhydrogenase are catalytically active in an alternating fashion according to a previously proposed half-of-the-sites reactivity model.
Subject headings and genre
Added entries (persons, corporate bodies, meetings, titles ...)
-
Ahnström, G
(author)
-
Rydström, J
(author)
-
Department of Biochemistry, Arrhenius Laboratory, University of Stockholm
(creator_code:org_t)
Related titles
-
In:Archives of Biochemistry and Biophysics: Elsevier BV259:2, s. 341-3490003-98611096-0384
Internet link
Find in a library
To the university's database