Solubilization of human bombesin/GRP receptors
- George Washington Univ., Washington, DC (United States)
Bombesin/gastrin releasing peptide (BN/GRP) functions as a growth factor in certain tumors. Recently, the authors found the human glioblastoma cell line U-118 binds radiolabeled (Tyr{sup 4})bombesin (BN) with high affinity (Kd = 2 nM) to a single class of sites (Bmax = 30,000/cell). Using 1 mM disuccinimidyl suberate, {sup 125}I-GRP was cross-linked to a 75 Kdalton protein using U-118 cells. Here the human BN/GRP receptor was solubilized and characterized biochemically. The data indicate that the C-terminal octapeptide of NB/GRP is essential for high affinity binding to the human BN/GRP receptor. Because the solubilized receptor has an apparent molecular weight of 200 Kdaltons using gel filtration techniques, it may be an oligomeric protein.
- OSTI ID:
- 6062405
- Report Number(s):
- CONF-9104107-; CODEN: FAJOE
- Journal Information:
- FASEB Journal (Federation of American Societies for Experimental Biology); (United States), Vol. 4:3; Conference: 75. annual meeting of the Federation of American Societies for Experimental Biology (FASEB), Atlanta, GA (United States), 21-25 Apr 1991; ISSN 0892-6638
- Country of Publication:
- United States
- Language:
- English
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TUMOR CELLS
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550201* - Biochemistry- Tracer Techniques