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Monoamine oxidase (MAO), an important enzyme for the degradation of amine neurotransmitters, has been implicated in neu-ropsychiatric illness. The amino acid sequence for one form of the enzyme, MAO-A, has been deduced from human cDNA clones and verified against proteolytic peptides. The covalent binding site for the flavin adenine dinucleotide (FAD) cofactor is near the C-terminal region. The presence of features characteristic of the ADP-binding fold suggests that the N-terminal region is also involved in the binding of FAD. These cDNAs should facilitate the study of the structure, function, and intracellular targeting of MAO, as well as the analysis of its expression in normal and pathological states.

IT has been observed that in the study of patients hospitalized for investigation of liver or gall-bladder disease, or both, studies of bromsulfalein excretion and cholecystography are often done concomitantly. In the usual manner this implies the administration of an iodine dye for the cholecystogram on the night before x-ray studies and the addition of a bromine-containing compound (bromsulfalein) on the next morning. On a number of occasions we have noted that the bromsulfalein retention measured in this fashion is frequently out of proportion to existing liver disease, and with repeated determinations at a later date, the values have shown . . .