Insulin activates guanosine 5′-[γ-thio] triphosphate (GTPγS) binding to a novel GTP-binding protein, GIR, from human placenta

Satish Srivastava, Ugra S. Singh

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

A novel GTP-binding protein, GIR, along with insulin receptor (IR), has been partially purified from human placenta. A non-hydrolyzable substrate, GTPγS which is known to bind to GTP-binding proteins with high affinity, reduces insulin binding to IR-GIR fraction by approximately 29% and 100 nM insulin stimulates GTPγS binding to IR-GIR fraction by approximately five-fold. The molecular weight of the protein (may be subunit) that binds to 8-azido-GTP, a photoaffinity label for G-proteins, is approximately 66,000.

Original languageEnglish (US)
Pages (from-to)501-506
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume173
Issue number2
DOIs
StatePublished - Dec 14 1990

Fingerprint

Guanosine
Insulin Receptor
GTP-Binding Proteins
Placenta
Insulin
Photoaffinity Labels
Molecular Weight
Molecular weight
Substrates
triphosphoric acid
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Insulin activates guanosine 5′-[γ-thio] triphosphate (GTPγS) binding to a novel GTP-binding protein, GIR, from human placenta. / Srivastava, Satish; Singh, Ugra S.

In: Biochemical and Biophysical Research Communications, Vol. 173, No. 2, 14.12.1990, p. 501-506.

Research output: Contribution to journalArticle

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