Abstract
Monase indole-3(2-aminobu-tyl) acetate, a monoamine oxidase inhibitor, and 8 other structurally related compounds with different substitutions on the indole ring and amine side chain inhibited 5-HT uptake by platelets, degree of inhibition being directly related to concentration of inhibitor without particular relation to structure. C14-Mon-ase which differs from 5-HT by the absence of a hydroxyl group in position 5 of the indole ring and by the presence of a different side chain, was concentrated only slightly by platelets. It was concluded that the structural specificity for 5-HT uptake is largely determined by the hydroxyl group at position 5 of the indole ring.
Original language | English (US) |
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Pages (from-to) | 711-714 |
Number of pages | 4 |
Journal | Proceedings of the Society for Experimental Biology and Medicine |
Volume | 122 |
Issue number | 3 |
DOIs | |
State | Published - Jul 1966 |
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)