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Peptide bombesin

IC5Q — 3.4 pM gastrin-releasing peptide/bombesin receptor... [Pg.7]

Miscellaneous Peptides Bombesin Bradykinin Carnosine Neuropeptide Y Neurotensin Delta sleep factor Galanin Oxerin... [Pg.20]

Naldini, L., D. Cirillo, T. W. Moody, P. M. Comoglio, J. Schlessinger and R. Kris (1990). Solubilization of the receptor for the neuropeptide gastrin-releasing peptide (bombesin) with functional ligand binding properties. Biochemistry 29(21) 5153— 5160. [Pg.128]

Glucagon, cholacyatokinin, glucagon-like peptides, bombesin peptides, glucose... [Pg.83]

Specific peptide (bombesin, glucagon, etc.) may supplement the preceding studies. [Pg.227]

Bombesin family, a subfamily of the bombesin-like family to which belong bombesin, alytensin and gastrinreleasing peptide, a mammalian counterpart for bombesin. The amphibian peptides bombesin and alytensin are structurally very similar and display biological effects when applied to mammals, such as hypertensive action, stimulation of the uterus and digestive tract, hyperglycemic effect, stimulation on the gastric secretion and increase of insulin levels in peripheral blood. [Pg.50]

FIGURE 3.5 The calibration curve to determine mobilities of doubly protonated peptides bombesin, angiotensin II, and substance P, as well as quadruply protonated melittin. In the diagram full circles indicate the values obtained from internal calibrant peptides. These were angiotensin I + 3H+, bradykinin + 2H+, fibrinopeptide A + 2H, fibrinopeptide A + 3H neurotensin + 3H+, and GRGDS + H+. [Pg.63]

Simultaneous angiotensin I, angiotensin II, angiotensin III, atrial natriuretic peptide, bombesin, bradykinin, gonadorelin (LHRH), somatoliberin, vasopressin... [Pg.13]

Bombesin peptide Bombesin was conjugated to JV-acetyl histidine-modified GC for targeting gastric-releasing peptide receptors overexpressed in prostate cancer cells. Iron oxide was loaded to be tested as a probe for MRI [34]... [Pg.145]

The basic polymer appears to be a hydroxylated polyether to which octadecyl chains have been bonded and so it behaves as a reverse phase exhibiting dispersive interactions with the solutes. An example of the separation of a series of peptides is shown in figure 15. The column was 3.5 cm long, 4.6 mm i.d. The solutes shown were (1) oc-endorphin, (2) bombesin, (3) y-endorphin, (4) angiotensin, (5) somatostatin and (6) calcitonon. The separation was carried out with a 10 min linear program from water containing 0.2% trifluoroacetic acid to 80% acetonitrile. [Pg.90]

Finally, RNA editing can be involved, as in the case of the amphibian bombesin-like peptides, where nucleotides in the mRNA are changed and the final protein is not a direct reflection of the sequence encoded in the gene. RNA editing is also seen in the glutamate (Ch. 15) and serotonin receptors (Ch. 13 and Ch. 15) and probably will be found elsewhere as detection methods become more sophisticated. [Pg.326]

Aziridine cleavage based on an Sn2 reaction was used for the synthesis of peptides bearing E alkene dipeptide isosteres, a novel class of potent bombesin receptor antagonists [62]. Treatment of the vinylaziridine 86 (Scheme 9.19) with isobutyl and isopentyl magnesiocyanocuprates in THF at —78 °C for 30 min. stereospecifi-cally gave the desired E alkene isosteres 87 in high isolated yields [63]. [Pg.305]

Semi-rational approaches Four subt)rpes of the bombesin receptor have been identified (gastrin-releasing peptide [GRP] receptor, neuromedin B receptor, the orphan receptor bombesin receptor subtype 3 and bombesin receptor subtype 4). The roles of individual receptor... [Pg.37]


See other pages where Peptide bombesin is mentioned: [Pg.6]    [Pg.29]    [Pg.221]    [Pg.223]    [Pg.53]    [Pg.191]    [Pg.182]    [Pg.206]    [Pg.186]    [Pg.101]    [Pg.308]    [Pg.152]    [Pg.6]    [Pg.29]    [Pg.221]    [Pg.223]    [Pg.53]    [Pg.191]    [Pg.182]    [Pg.206]    [Pg.186]    [Pg.101]    [Pg.308]    [Pg.152]    [Pg.530]    [Pg.219]    [Pg.123]    [Pg.124]    [Pg.305]    [Pg.276]    [Pg.276]    [Pg.525]    [Pg.828]    [Pg.908]    [Pg.1488]    [Pg.66]    [Pg.6]    [Pg.247]    [Pg.1095]    [Pg.138]    [Pg.139]    [Pg.147]    [Pg.28]    [Pg.467]    [Pg.297]    [Pg.267]    [Pg.38]    [Pg.61]   
See also in sourсe #XX -- [ Pg.66 ]




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