Purification and characterization of the head-activator receptor from a multi-headed mutant of Chlorohydra viridissima.

Abstract:

:In hydra the neuropeptide head activator (HA) is responsible for head-specific growth and differentiation processes. The effects of HA are mediated by high and low affinity receptors on hydra cells. In the current study HA receptors from a multi-headed mutant of Chlorohydra viridissima were solubilized from the membrane fraction using 1% Triton X-100 and 2.5 M urea. Scatchard analysis showed that the solubilized receptor had a Kd of 1.55 x 10(-9) M, indicating the low affinity subtype of the HA receptor. The solubilized receptor was purified by DMAE chromatography and subsequent affinity chromatography to homogeneity. SDS-PAGE revealed a single protein band with a molecular mass of 96 +/- 4 kDa. The native receptor eluted during gel filtration as a 113 kDa protein, and focussed with an isoelectric point of 4.8.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Christians S,Neubauer KH,Ulrich H

doi

10.1016/0014-5793(93)81203-c

subject

Has Abstract

pub_date

1993-01-25 00:00:00

pages

141-6

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(93)81203-C

journal_volume

316

pub_type

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