Antibodies against the carboxyl-terminal 5-kDa peptide of the α subunit of transducin crossreact with the 40-kDa but not the 39-kDa guanine nucleotide binding protein from brain

M. Pines, P. Gierschik, G. Milligan, W. Klee, Allen M. Spiegel

Research output: Contribution to journalArticle

55 Citations (Scopus)

Abstract

We tested 18 antisera showing reactivity against the α subunit of transducin, the guanine nucleotide binding protein from rod outer segment, for crossreactivity against the 40- and 39-kDa guanine nucleotide binding proteins purified from bovine brain. A single antiserum, CW6, showed crossreactivity, and this was predominantly against the 40-kDa protein. Immunoblots of the tryptic fragments of transducin α subunit with multiple antisera raised against that subunit showed that only CW6 recognizes a COOH-terminal 5-kDa peptide that includes the site of pertussis toxin ADP-ribosylation. Antibodies against the 5-kDa peptide, affinity-purified from CW6, specifically react with the 40-kDa brain protein on immunoblots. The results show that the 39- and 40-kDa guanine nucleotide binding proteins from brain differ immunochemically and that the COOH-terminal 5-kDa peptide of transducin α subunit is homologous to a region in the 40-kDa brain protein. We speculate that this homologous region may be in a domain that confers specificity for receptor interactions of guanine nucleotide binding proteins.

Original languageEnglish (US)
Pages (from-to)4095-4099
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume82
Issue number12
DOIs
StatePublished - 1985
Externally publishedYes

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Transducin
Guanine Nucleotides
Carrier Proteins
Immune Sera
Peptides
Antibodies
Brain
Rod Cell Outer Segment
Proteins
Pertussis Toxin
Adenosine Diphosphate

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

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title = "Antibodies against the carboxyl-terminal 5-kDa peptide of the α subunit of transducin crossreact with the 40-kDa but not the 39-kDa guanine nucleotide binding protein from brain",
abstract = "We tested 18 antisera showing reactivity against the α subunit of transducin, the guanine nucleotide binding protein from rod outer segment, for crossreactivity against the 40- and 39-kDa guanine nucleotide binding proteins purified from bovine brain. A single antiserum, CW6, showed crossreactivity, and this was predominantly against the 40-kDa protein. Immunoblots of the tryptic fragments of transducin α subunit with multiple antisera raised against that subunit showed that only CW6 recognizes a COOH-terminal 5-kDa peptide that includes the site of pertussis toxin ADP-ribosylation. Antibodies against the 5-kDa peptide, affinity-purified from CW6, specifically react with the 40-kDa brain protein on immunoblots. The results show that the 39- and 40-kDa guanine nucleotide binding proteins from brain differ immunochemically and that the COOH-terminal 5-kDa peptide of transducin α subunit is homologous to a region in the 40-kDa brain protein. We speculate that this homologous region may be in a domain that confers specificity for receptor interactions of guanine nucleotide binding proteins.",
author = "M. Pines and P. Gierschik and G. Milligan and W. Klee and Spiegel, {Allen M.}",
year = "1985",
doi = "10.1073/pnas.82.12.4095",
language = "English (US)",
volume = "82",
pages = "4095--4099",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
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TY - JOUR

T1 - Antibodies against the carboxyl-terminal 5-kDa peptide of the α subunit of transducin crossreact with the 40-kDa but not the 39-kDa guanine nucleotide binding protein from brain

AU - Pines, M.

AU - Gierschik, P.

AU - Milligan, G.

AU - Klee, W.

AU - Spiegel, Allen M.

PY - 1985

Y1 - 1985

N2 - We tested 18 antisera showing reactivity against the α subunit of transducin, the guanine nucleotide binding protein from rod outer segment, for crossreactivity against the 40- and 39-kDa guanine nucleotide binding proteins purified from bovine brain. A single antiserum, CW6, showed crossreactivity, and this was predominantly against the 40-kDa protein. Immunoblots of the tryptic fragments of transducin α subunit with multiple antisera raised against that subunit showed that only CW6 recognizes a COOH-terminal 5-kDa peptide that includes the site of pertussis toxin ADP-ribosylation. Antibodies against the 5-kDa peptide, affinity-purified from CW6, specifically react with the 40-kDa brain protein on immunoblots. The results show that the 39- and 40-kDa guanine nucleotide binding proteins from brain differ immunochemically and that the COOH-terminal 5-kDa peptide of transducin α subunit is homologous to a region in the 40-kDa brain protein. We speculate that this homologous region may be in a domain that confers specificity for receptor interactions of guanine nucleotide binding proteins.

AB - We tested 18 antisera showing reactivity against the α subunit of transducin, the guanine nucleotide binding protein from rod outer segment, for crossreactivity against the 40- and 39-kDa guanine nucleotide binding proteins purified from bovine brain. A single antiserum, CW6, showed crossreactivity, and this was predominantly against the 40-kDa protein. Immunoblots of the tryptic fragments of transducin α subunit with multiple antisera raised against that subunit showed that only CW6 recognizes a COOH-terminal 5-kDa peptide that includes the site of pertussis toxin ADP-ribosylation. Antibodies against the 5-kDa peptide, affinity-purified from CW6, specifically react with the 40-kDa brain protein on immunoblots. The results show that the 39- and 40-kDa guanine nucleotide binding proteins from brain differ immunochemically and that the COOH-terminal 5-kDa peptide of transducin α subunit is homologous to a region in the 40-kDa brain protein. We speculate that this homologous region may be in a domain that confers specificity for receptor interactions of guanine nucleotide binding proteins.

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U2 - 10.1073/pnas.82.12.4095

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