Abstract:
:Two synthetic photoactive azidoarylphosphatidylcholines were used to investigate the level of interaction between D-beta-hydroxybutyrate apodehydrogenase (apoBDH), an amphipathic membrane protein, with the hydrophobic domain of phospholipids. The two synthetic lecithins, PL I (1-myristoyl-2-12-N-(4-azido-2-nitrophenyl) aminododecanoyl-sn-glycero-3-phosphocholine) and PL II (1-myristoyl-2-(2-azido-4-nitrobenzoyl)-sn-glycero-3-phosphocholine), are able to reactivate the non-active purified apoBDH as well as the non-photoactive homologs, indicating that the photoreactive chemical groups are without effect on the cofactor properties of phosphatidylcholine. Photoirradiation of reconstituted complexes between phospholipid containing azidoaryllecithin and apoBDH leads to a covalent binding of some synthetic lecithin molecules on the protein. The labelling, about 3 times higher with PL II than with PL I, suggests that the area of interacting domain of BDH with the hydrophobic moiety of phospholipid is more important at or near the surface of the lipid bilayer than in the inner part. This approach is further demonstration that BDH is an integral protein.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
el Kebbaj MS,Berrez JM,Lakhlifi T,Morpain C,Latruffe Ndoi
10.1016/0014-5793(85)81178-9subject
Has Abstractpub_date
1985-03-11 00:00:00pages
176-80issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(85)81178-9journal_volume
182pub_type
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