guanylyl-imidodiphosphate and 8-azidoguanosine-triphosphate

guanylyl-imidodiphosphate has been researched along with 8-azidoguanosine-triphosphate* in 2 studies

Other Studies

2 other study(ies) available for guanylyl-imidodiphosphate and 8-azidoguanosine-triphosphate

Article	Year
Myelin basic protein binds GTP at a single site in the N-terminus. Biochemical and biophysical research communications, 1988, May-16, Volume: 152, Issue:3 Myelin basic protein from normal human brain was ADP-ribosylated with Cholera toxin, but not with Pertussis toxin. It bound azido-GTP at a single site in the N-terminal tetrapeptide at the Gln residue. The binding was considerably reduced when GppNHp was present during azido-GTP binding and totally inhibited when GTP gamma S was present. The relevance of this specific binding is not understood at this time. Topics: Adenosine Diphosphate Ribose; Amino Acids; Azides; Binding Sites; Cholera Toxin; Guanosine 5'-O-(3-Thiotriphosphate); Guanosine Triphosphate; Guanylyl Imidodiphosphate; Humans; Myelin Basic Protein; Pertussis Toxin; Thionucleotides; Virulence Factors, Bordetella	1988
Synthesis of 2',3'-O-(2,4,6-trinitrocyclohexadienylidine)guanosine 5'-triphosphate and a study of its inhibitory properties with adenylate cyclase. Archives of biochemistry and biophysics, 1986, Volume: 245, Issue:2 A fluorescent GTP analog 2',3'-O-(2,4,6-trinitrocyclohexadienylidine) guanosine 5'-triphosphate (TNP-GTP) has been prepared and some of its physical properties characterized. TNP-GTP was found to be a potent inhibitor of chick embryo heart adenylate cyclase as activated by guanyl 5'-(beta,gamma-imido)triphosphate (GppNHp), F-, and forskolin with Ki values in the 8-15 microM range. It also appeared to inhibit substantially basal adenylate cyclase in this system. TNP-GTP demonstrated an effective competition with [3H]GppNHp, binding to membranes equivalently to GppNHp and about three times better than GTP. 8-Azidoguanosine 5'-triphosphate (8N3GTP) mimics GTP activation of chick embryo heart adenylate cyclase and [gamma-32P]8N3GTP is effectively photoincorporated into a 42,000- to 44,000-Mr doublet when proteins are separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. TNP-GTP effectively prevents this photoincorporation, as does GTP, at concentrations that agree with their respective apparent inhibition and activation binding constants. The data suggest that TNP-GTP could prove to be a valuable tool for studying the mechanisms of GTP regulation of adenylate cyclase and other GTP-regulated systems. Topics: Adenylyl Cyclase Inhibitors; Alkaline Phosphatase; Animals; Azides; Binding, Competitive; Chemical Phenomena; Chemistry; Chick Embryo; Colforsin; Enzyme Activation; Guanosine Triphosphate; Guanylyl Imidodiphosphate; Hydrogen-Ion Concentration; Myocardium; Photochemistry; Sodium Fluoride; Spectrophotometry	1986

Article

Year

Myelin basic protein binds GTP at a single site in the N-terminus.

Biochemical and biophysical research communications, 1988, May-16, Volume: 152, Issue:3

Myelin basic protein from normal human brain was ADP-ribosylated with Cholera toxin, but not with Pertussis toxin. It bound azido-GTP at a single site in the N-terminal tetrapeptide at the Gln residue. The binding was considerably reduced when GppNHp was present during azido-GTP binding and totally inhibited when GTP gamma S was present. The relevance of this specific binding is not understood at this time.

Topics: Adenosine Diphosphate Ribose; Amino Acids; Azides; Binding Sites; Cholera Toxin; Guanosine 5'-O-(3-Thiotriphosphate); Guanosine Triphosphate; Guanylyl Imidodiphosphate; Humans; Myelin Basic Protein; Pertussis Toxin; Thionucleotides; Virulence Factors, Bordetella

1988

Synthesis of 2',3'-O-(2,4,6-trinitrocyclohexadienylidine)guanosine 5'-triphosphate and a study of its inhibitory properties with adenylate cyclase.

Archives of biochemistry and biophysics, 1986, Volume: 245, Issue:2

A fluorescent GTP analog 2',3'-O-(2,4,6-trinitrocyclohexadienylidine) guanosine 5'-triphosphate (TNP-GTP) has been prepared and some of its physical properties characterized. TNP-GTP was found to be a potent inhibitor of chick embryo heart adenylate cyclase as activated by guanyl 5'-(beta,gamma-imido)triphosphate (GppNHp), F-, and forskolin with Ki values in the 8-15 microM range. It also appeared to inhibit substantially basal adenylate cyclase in this system. TNP-GTP demonstrated an effective competition with [3H]GppNHp, binding to membranes equivalently to GppNHp and about three times better than GTP. 8-Azidoguanosine 5'-triphosphate (8N3GTP) mimics GTP activation of chick embryo heart adenylate cyclase and [gamma-32P]8N3GTP is effectively photoincorporated into a 42,000- to 44,000-Mr doublet when proteins are separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. TNP-GTP effectively prevents this photoincorporation, as does GTP, at concentrations that agree with their respective apparent inhibition and activation binding constants. The data suggest that TNP-GTP could prove to be a valuable tool for studying the mechanisms of GTP regulation of adenylate cyclase and other GTP-regulated systems.

Topics: Adenylyl Cyclase Inhibitors; Alkaline Phosphatase; Animals; Azides; Binding, Competitive; Chemical Phenomena; Chemistry; Chick Embryo; Colforsin; Enzyme Activation; Guanosine Triphosphate; Guanylyl Imidodiphosphate; Hydrogen-Ion Concentration; Myocardium; Photochemistry; Sodium Fluoride; Spectrophotometry

1986