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J. Biol. Chem., Vol. 263, Issue 1, 144-149, Jan, 1988
J Mazella, J Chabry, P Kitabgi and JP Vincent
Neurotensin receptors were solubilized from mouse brain using the
zwitterionic detergent 3-[(3-cholamidopropyl)dimethylammonio]-1-
propanesulfonic acid (CHAPS). The binding of 125I-labeled [Tyr3]neurotensin
to the soluble fraction was time-dependent, saturable, and reversible.
Unlabeled neurotensin and its analogues acetylneurotensin (8-13),
neurotensin (9-13), and neurotensin (1-12) competitively antagonized the
binding of 125I-labeled [Tyr3]neurotensin to CHAPS-solubilized extracts
with relative potencies similar to those observed with membrane-bound
receptors. Scatchard analysis of equilibrium binding data indicated that
the soluble extract contained a single class of neurotensin binding sites
with a Kd of 0.36 nM and a Bm of 63 fmol/mg. As already observed with
membrane-bound receptors, the affinity of neurotensin for the soluble
binding activity was decreased by Na+ ions. By contrast, soluble receptors
were no longer sensitive to GTP and the antihistamine drug levocabastine. A
molecular weight of about 100,000 was determined for soluble neurotensin
receptors both under native conditions by gel filtration on Ultrogel AcA 34
and under denaturating conditions by sodium dodecyl sulfate-polyacrylamide
gel electrophoresis after photoaffinity labeling.
Solubilization and characterization of active neurotensin receptors from mouse brain
Centre de Biochimie, Universite de Nice, Faculte des Sciences, France.
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