Purification of L-( sup 3 H) Nicotine eliminates low affinity binding

Journal Article · Mon Jan 01 00:00:00 EST 1990 · Life Sciences; (USA)

DOI:https://doi.org/10.1016/0024-3205(90)90095-9· OSTI ID:7138233

Romm, E; Marks, M J; Collins, A C ^[1]; Lippiello, P M ^[2]

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1. Univ. of Colorado, Boulder (USA)
2. R.J. Reynolds Tobacco Co., Winston Salem, NC (USA)

Some studies of L-({sup 3}H) nicotine binding to rodent and human brain tissue have detected two binding sites as evidenced by nonlinear Scatchard plots. Evidence presented here indicated that the low affinity binding site is not stereospecific, is not inhibited by low concentrations of cholinergic agonists and is probably due to breakdown products of nicotine since purification of the L-({sup 3}H)nicotine eliminates the low affinity site.

• OSTI ID: 7138233
• Journal Information: Life Sciences; (USA), Vol. 46:13; ISSN 0024-3205
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
NICOTINE
BIOCHEMICAL REACTION KINETICS
AFFINITY
FRACTIONATION
MAN
RECEPTORS
RODENTS
TRACER TECHNIQUES
TRITIUM COMPOUNDS
ALKALOIDS
AMINES
ANIMALS
AUTONOMIC NERVOUS SYSTEM AGENTS
AZINES
AZOLES
DRUGS
HETEROCYCLIC COMPOUNDS
HYDROGEN COMPOUNDS
ISOTOPE APPLICATIONS
KINETICS
MAMMALS
MEMBRANE PROTEINS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
PARASYMPATHOLYTICS
PARASYMPATHOMIMETICS
PRIMATES
PROTEINS
PYRIDINES
PYRROLES
PYRROLIDINES
REACTION KINETICS
SEPARATION PROCESSES
VERTEBRATES
550201* - Biochemistry- Tracer Techniques