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Isolation of a Housefly Head Protein Fraction that Exhibits High Affinity Binding of Cholinergic Ligands

Philip J. Jewess ; Woodstock Laboratory, Sittingbourne Research Centre, SheU Research Limited, Sittingbourne ME9 SAG, Kent, U.K.
Barry S. Clarke ; Woodstock Laboratory, Sittingbourne Research Centre, SheU Research Limited, Sittingbourne ME9 SAG, Kent, U.K.
John F. Donnellan ; Woodstock Laboratory, Sittingbourne Research Centre, SheU Research Limited, Sittingbourne ME9 SAG, Kent, U.K.


Puni tekst: engleski pdf 5.506 Kb

str. 459-464

preuzimanja: 243

citiraj


Sažetak

The purification is described of a protein fraction, isolated from
the central nervous system of housefly heads, that exhibits high
affinity for cholinergic ligands. The purified material was found tq
bind with high affinity acetylcholine, nicotinic ligands such as
nicotine and decamethonium as well as atropine, dexetimide a:qg
pilocarpine which are of a muscarinic nature. With all the ligands
there appeared to be only a single site for binding with measured
dissociation constants varying from 6.2 X 10-s M (dexetimide) to
5.4 x 10-6 M (pilocarpine). The concentration of binding sites was
in the range of 381 nmol g-1 of protein (atropine) to 560 nmol g-1
of protein (pilocarpine).

Ključne riječi

Hrčak ID:

196640

URI

https://hrcak.srce.hr/196640

Datum izdavanja:

3.12.1975.

Posjeta: 633 *