[Quantitative approach to the interactions of D-beta-hydroxybuturate dehydrogenase with phospholipids]

Depending on the basis of the technique used, an estimation of 2 to 6 lecithin molecules are required for reactivation of purified D-beta-hydroxybutyrate apodehydrogenase (apoBDH). 60 to 70 mitochondrial phospholipid molecules are necessary for insertion of one BDH polypeptide chain where 16 molecules would be in direct interaction with the enzyme. Results show off the cofactor role of lecithin and also the requirement of an amphiphilic environment, essential for the enzyme function.