RT Journal Article
SR Electronic
T1 THE DEACETYLATION OF HEROIN AND RELATED COMPOUNDS BY MAMMALIAN TISSUES
JF Journal of Pharmacology and Experimental Therapeutics
JO J Pharmacol Exp Ther
FD American Society for Pharmacology and Experimental Therapeutics
SP 328
OP 337
VO 75
IS 3
A1 C. I. WRIGHT
YR 1942
UL http://jpet.aspetjournals.org/content/75/3/328.abstract
AB Mammalian tissues (human, rabbit, and rat) contain an enzyme or enzymes capable of deacetylating heroin and dihydroheroin at both the 3-carbon and 6-carbon positions. Of the tissues examined, liver has the highest concentration of this enzymic activity followed, in general, by kidney, brain, blood serum, and muscle. Dihydroheroin is deacetylated at a slower rate per unit of tissue than heroin and the 6-carbon acetyl is removed from both at a much slower rate than the 3-carbon acetyl. Rabbit liver has a greater capacity for deacetylation at the 3-carbon position, than rat or human liver while human liver deacetylates at the 6-carbon position more rapidly than rabbit or rat liver. There is some evidence that the enzyme that catalyzes the hydrolysis of atropine also catalyzes the hydrolysis of monoacetylmorphine or the hydrolysis of heroin at the 6-carbon position.