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Biochem Pharmacol. 1996 Jun 14;51(11):1521-5.

Redox cycling activity of monoamine-serotonin binding protein conjugates.

Author information

1
Department of Protein Chemistry, Free University of Brussels (VUB), St. Genesius-Rode, Belgium.

Abstract

It has been shown recently that the covalent binding of labelled dopamine and serotonin to serotonin binding proteins (SBP) from bovine frontal cortex is potently inhibited by their related neurotoxins. The present study reveals that the monoamine-SBP conjugates of serotonin, dopamine, and related toxins are able to catalyse redox cycling reactions. Using an improved method to detect quinoproteins in SDS-PAGE gels, we were also able to demonstrate that the redox cycling activity corresponded to two major protein components with molecular weights of 45 and 56 kDa. The covalent monoamine-SBP conjugates may be referred to as "artificial quinoproteins."

PMID:
8630093
DOI:
10.1016/0006-2952(96)00093-7
[Indexed for MEDLINE]

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