Substrate binding sites of monoamine oxidase as studied by 4-fluoro-3-nitrophenyl azide

Book · Wed Jan 01 04:00:00 EST 1986

OSTI ID:5348800

Hsu, M C

Monoamine oxidase (MAO) is a flavin-adenine dinucleotide (FAD)-containing enzyme. This enzyme degrades a number of biogenic amines and may be related to the etiology of psychiatric disorders and may other diseases. Better understanding of the chemical nature and molecular basis of MAO will help to better understand the diseases associated with this enzyme. 4-Fluoro-3-nitrophenyl azide (FNPA), a photoaffinity probe, has been shown to be useful for investigating binding sites on macromolecules. The objectives of this study are: (1) to investigate the effect of FNPA on human brain cortex MAO, human placental MAO, and beef liver MAO in the dark and following photolysis; (2) to characterize the (/sup 3/H)-FNPA binding site on purified beef liver MAO-B; (3) to determine the sequence of FNPA-labeled peptides from the active site of MAO-B; and (4) to elicit an antibody against beef liver MAO-B.

• Research Organization: South Carolina Univ., Columbia (USA)
• OSTI ID: 5348800
• Country of Publication: United States
• Language: English

Related Subjects

550201* -- Biochemistry-- Tracer Techniques
550901 -- Pathology-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
AMINO ACID SEQUENCE
ANIMALS
AZIDES
BODY
BRAIN
CATTLE
CENTRAL NERVOUS SYSTEM
CHEMICAL COMPOSITION
CHEMICAL REACTIONS
DECOMPOSITION
DIGESTIVE SYSTEM
DOMESTIC ANIMALS
ENZYMES
ETIOLOGY
FETAL MEMBRANES
GLANDS
ISOTOPE APPLICATIONS
LABELLED COMPOUNDS
LIVER
MAMMALS
MAN
MEMBRANE PROTEINS
MEMBRANES
MENTAL DISORDERS
MOLECULAR BIOLOGY
MOLECULAR STRUCTURE
NERVOUS SYSTEM
NITROGEN COMPOUNDS
ORGANIC COMPOUNDS
ORGANS
OXIDOREDUCTASES
PHOTOCHEMICAL REACTIONS
PHOTOLYSIS
PLACENTA
PRIMATES
PROTEINS
RECEPTORS
RUMINANTS
SUBSTRATES
TRACER TECHNIQUES
TRITIUM COMPOUNDS
VERTEBRATES