Characterization of a membrane-associated, receptor and G-protein responsive Phosphoinositide-specific Phospholipase C from avian erythrocytes

  1. Ruiz-Larrea, F. 2
  2. Berrie, C.P. 1
  1. 1 University of Liverpool
    info

    University of Liverpool

    Liverpool, Reino Unido

    ROR https://ror.org/04xs57h96

  2. 2 Centro Nacional de Biotecnología
    info

    Centro Nacional de Biotecnología

    Madrid, España

    ROR https://ror.org/015w4v032

Revista:
FEBS Letters

ISSN: 0014-5793

Año de publicación: 1993

Volumen: 328

Número: 1-2

Páginas: 174-182

Tipo: Artículo

DOI: 10.1016/0014-5793(93)80988-7 PMID: 8393807 SCOPUS: 2-s2.0-0027293268 GOOGLE SCHOLAR

Otras publicaciones en: FEBS Letters

Repositorio institucional: lock_openAcceso abierto Editor

Resumen

We describe the reconstitution and purification of a membrane-associated phosphoinositide-specific phospholipase C (PIC) from turkey erythrocyte ghosts. This PIC is responsive to a G-protein coupled to P(2y) purinergic receptors which are expressed in turkey erythrocytes. Reconstitution is achieved by adding partially purified PIC to [ 3H]inositol-prelabelled turkey erythrocyte membranes depleted of their endogenous PIC (acceptor membranes). PIC activity is associated with a 52 kDa polypeptide on SDS-polyacrylamide gel electrophoresis. Addition of a 307-fold purified enzyme to the acceptor membranes has no effect on basal PIC activity, but markedly increases the response to GTPγS and P(2y)-purinergic receptor activation.