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Hemicholinum-3 binding sites in the nervous tissue of insects.

Abstract：

:High-affinity binding sites for tritiated hemicholinium-3, a potent and selective inhibitor of the sodium-dependent high-affinity choline transport, have been found in synaptosomal membranes from insect ganglia. The binding of hemicholinium to ganglionic membrane preparations was saturable and specific with an apparent K(D) of about 8 nM and a B(max) of 1250 fmol/mg protein. Maximal binding occurred only in the presence of sodium chloride. Upon u.v.-illumination, tritiated hemicholinium-3 appeared to be irreversibly crosslinked to its specific binding sites. Subsequent analysis on SDS-polyacrylamide gels revealed that a single polypeptide band, corresponding to an apparent molecular mass of about 80,000, was labelled.

journal_name

Neurochem Int

journal_title

Neurochemistry international

authors

Knipper M,Krieger J,Breer H

doi

10.1016/0197-0186(89)90124-1

subject

Has Abstract

pub_date

1989-01-01 00:00:00

pages

211-5

issue

2

eissn

0197-0186

issn

1872-9754

pii

0197-0186(89)90124-1

journal_volume

14

pub_type

杂志文章

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