TY - JOUR
T1 - Insulin activates guanosine 5′-[γ-thio] triphosphate (GTPγS) binding to a novel GTP-binding protein, GIR, from human placenta
AU - Srivastava, Satish K.
AU - Singh, Ugra S.
N1 - Funding Information:
We gratefully acknowledge the valuable discussion with Dr. Charles A. Stuart, Department of Internal Medicine, UTMB. This work was supported in part by NIH Grants EY-01677 and DK-36118.
PY - 1990/12/14
Y1 - 1990/12/14
N2 - 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.
AB - 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.
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U2 - 10.1016/S0006-291X(05)80062-2
DO - 10.1016/S0006-291X(05)80062-2
M3 - Article
C2 - 2124484
AN - SCOPUS:0025685604
SN - 0006-291X
VL - 173
SP - 501
EP - 506
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -