Antibodies against a retinal guanine nucleotide-binding protein cross-react with a single plasma membrane protein in non-retinal tissues

Peter Gierschik, Cyrena Simons, Charles Woodard, Robert Somers, Allen M. Spiegel

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

Antisera (AS/1-AS/6) to purified bovine retinal transducin, a guanine nucleotide-binding protein, were produced in 6 rabbits. Immunoblots showed that the antisera varied in their reactivity with the subunits of transducin; AS/1 reacted strongly with all 3 subunits, while the others reacted with only the β and/or γ subunits. Only AS/1 specifically immunoprecipitated the α subunit radiolabeled with non-covalently bound guanine nucleotides. Immunostaining of plasma membrane proteins from non-retinal tissues with AS-1 revealed a single protein (approx. 35 kDa), most likely representing the β subunit of the guanine nucleotide-binding proteins (Gs and gi associated with adenylate cyclase. Cerebral cortex showed the highest content of this protein. Antisera against transducin provide a highly specific and sensitive probe for quantitation of the β subunit of Gs and Gi.

Original languageEnglish (US)
Pages (from-to)321-325
Number of pages5
JournalFEBS Letters
Volume172
Issue number2
DOIs
StatePublished - Jul 9 1984
Externally publishedYes

Fingerprint

Transducin
Guanine Nucleotides
Cell membranes
Blood Proteins
Immune Sera
Carrier Proteins
Membrane Proteins
Cell Membrane
Tissue
Antibodies
Adenylyl Cyclases
Cerebral Cortex
Proteins
Rabbits

Keywords

  • Adenylate cyclase
  • Guanine nucleotide-binding protein
  • Retina
  • Rod outer segment membrane

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Antibodies against a retinal guanine nucleotide-binding protein cross-react with a single plasma membrane protein in non-retinal tissues. / Gierschik, Peter; Simons, Cyrena; Woodard, Charles; Somers, Robert; Spiegel, Allen M.

In: FEBS Letters, Vol. 172, No. 2, 09.07.1984, p. 321-325.

Research output: Contribution to journalArticle

Gierschik, Peter ; Simons, Cyrena ; Woodard, Charles ; Somers, Robert ; Spiegel, Allen M. / Antibodies against a retinal guanine nucleotide-binding protein cross-react with a single plasma membrane protein in non-retinal tissues. In: FEBS Letters. 1984 ; Vol. 172, No. 2. pp. 321-325.
@article{70f36033bb264d7f999c7962943ac19d,
title = "Antibodies against a retinal guanine nucleotide-binding protein cross-react with a single plasma membrane protein in non-retinal tissues",
abstract = "Antisera (AS/1-AS/6) to purified bovine retinal transducin, a guanine nucleotide-binding protein, were produced in 6 rabbits. Immunoblots showed that the antisera varied in their reactivity with the subunits of transducin; AS/1 reacted strongly with all 3 subunits, while the others reacted with only the β and/or γ subunits. Only AS/1 specifically immunoprecipitated the α subunit radiolabeled with non-covalently bound guanine nucleotides. Immunostaining of plasma membrane proteins from non-retinal tissues with AS-1 revealed a single protein (approx. 35 kDa), most likely representing the β subunit of the guanine nucleotide-binding proteins (Gs and gi associated with adenylate cyclase. Cerebral cortex showed the highest content of this protein. Antisera against transducin provide a highly specific and sensitive probe for quantitation of the β subunit of Gs and Gi.",
keywords = "Adenylate cyclase, Guanine nucleotide-binding protein, Retina, Rod outer segment membrane",
author = "Peter Gierschik and Cyrena Simons and Charles Woodard and Robert Somers and Spiegel, {Allen M.}",
year = "1984",
month = "7",
day = "9",
doi = "10.1016/0014-5793(84)81149-7",
language = "English (US)",
volume = "172",
pages = "321--325",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "2",

}

TY - JOUR

T1 - Antibodies against a retinal guanine nucleotide-binding protein cross-react with a single plasma membrane protein in non-retinal tissues

AU - Gierschik, Peter

AU - Simons, Cyrena

AU - Woodard, Charles

AU - Somers, Robert

AU - Spiegel, Allen M.

PY - 1984/7/9

Y1 - 1984/7/9

N2 - Antisera (AS/1-AS/6) to purified bovine retinal transducin, a guanine nucleotide-binding protein, were produced in 6 rabbits. Immunoblots showed that the antisera varied in their reactivity with the subunits of transducin; AS/1 reacted strongly with all 3 subunits, while the others reacted with only the β and/or γ subunits. Only AS/1 specifically immunoprecipitated the α subunit radiolabeled with non-covalently bound guanine nucleotides. Immunostaining of plasma membrane proteins from non-retinal tissues with AS-1 revealed a single protein (approx. 35 kDa), most likely representing the β subunit of the guanine nucleotide-binding proteins (Gs and gi associated with adenylate cyclase. Cerebral cortex showed the highest content of this protein. Antisera against transducin provide a highly specific and sensitive probe for quantitation of the β subunit of Gs and Gi.

AB - Antisera (AS/1-AS/6) to purified bovine retinal transducin, a guanine nucleotide-binding protein, were produced in 6 rabbits. Immunoblots showed that the antisera varied in their reactivity with the subunits of transducin; AS/1 reacted strongly with all 3 subunits, while the others reacted with only the β and/or γ subunits. Only AS/1 specifically immunoprecipitated the α subunit radiolabeled with non-covalently bound guanine nucleotides. Immunostaining of plasma membrane proteins from non-retinal tissues with AS-1 revealed a single protein (approx. 35 kDa), most likely representing the β subunit of the guanine nucleotide-binding proteins (Gs and gi associated with adenylate cyclase. Cerebral cortex showed the highest content of this protein. Antisera against transducin provide a highly specific and sensitive probe for quantitation of the β subunit of Gs and Gi.

KW - Adenylate cyclase

KW - Guanine nucleotide-binding protein

KW - Retina

KW - Rod outer segment membrane

UR - http://www.scopus.com/inward/record.url?scp=0021165078&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021165078&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(84)81149-7

DO - 10.1016/0014-5793(84)81149-7

M3 - Article

VL - 172

SP - 321

EP - 325

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 2

ER -