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Serotonin binds specifically and saturably to an actin-like protein isolated from rat brain synaptosomes


Small, DH and Wurtman, RJ, Serotonin binds specifically and saturably to an actin-like protein isolated from rat brain synaptosomes, National Academy of Sciences of The United States of America. Proceedings, 81, (3) pp. 959-963. ISSN 0027-8424 (1984) [Refereed Article]

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Copyright 1984 National Academy of Sciences

DOI: doi:10.1073/pnas.81.3.959


A soluble serotonin-binding was identified in a high-speed supernatant fraction of an osmotically shocked rat brain synaptosome (P 2 ) preparation. The binding of serotonin was saturable (B(max) = 6.0 nmol per mg of protein) and was specific for serotonin and a few structurally related compounds including dopamine and norepinephrine. Binding of serotonin (1 μM) was inhibited ~40% by chlorpromazine (10 μM). The affinity of serotonin for the binding protein was low in the crude extract (k(d) = 1.7 x 10 -3 M). However, on purification by chromatography on a column of phenothiazine agarose, a higher affinity (K(d) = 10 -5 M) binding component was also observed. The purified protein was greatly enriched in a polypeptide of M(r) of 43,000 that comigrated on polyacrylamide gel with skeletal muscle actin. Muscle actin also bound serotonin, and the binding to actin was similar to that of the purified protein in both the specificity of the binding and the affinity for serotonin. It is likely that the serotonin-binding protein is identical to cytoplasmic G-actin or an actin-like protein of similar molecular weight.

Item Details

Item Type:Refereed Article
Research Division:Biological Sciences
Research Group:Biochemistry and cell biology
Research Field:Cell neurochemistry
Objective Division:Health
Objective Group:Clinical health
Objective Field:Clinical health not elsewhere classified
UTAS Author:Small, DH (Professor David Small)
ID Code:52867
Year Published:1984
Web of Science® Times Cited:23
Deposited By:Menzies Institute for Medical Research
Deposited On:2008-10-02
Last Modified:2012-05-01

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