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The thyrotropin-releasing hormone receptor from rat brain was solubilized in a stable unbound form. The natural glycoside digitonin was the only detergent of a variety tested capable of solubilizing the active receptor. The digitonin-solubilized receptor exhibited binding kinetics for 3-[3H]methylhistidine thyrotropin-releasing hormone virtually identical to membrane preparations and responded with a similar order of potency to a series of thyrotropin-releasing hormone analogues that inhibit binding of the labeled ligand. Gel filtration analysis and sucrose density gradient centrifugation indicated a Stokes radius of 5.2 nm, a sedimentation coefficient of 11.2 s, and a corresponding calculated molecular weight of 244,000 for the detergent-receptor complex. The soluble receptor shows a gradual loss of binding activity over 48 to 72 hr when kept at 4 degrees C. However, the preparation may be frozen at -20 degrees C with no significant loss of activity.
W A Johnson, and
N M Nathanson, and
A Horita
April 1989,
Molecular pharmacology,
W A Johnson, and
N M Nathanson, and
A Horita
July 1978,
Biochimica et biophysica acta,
W A Johnson, and
N M Nathanson, and
A Horita
May 1982,
Life sciences,
W A Johnson, and
N M Nathanson, and
A Horita
January 1986,
Science (New York, N.Y.),
W A Johnson, and
N M Nathanson, and
A Horita
April 1979,
Biochemistry,
W A Johnson, and
N M Nathanson, and
A Horita
January 1982,
Peptides,
W A Johnson, and
N M Nathanson, and
A Horita
December 1987,
Molecular endocrinology (Baltimore, Md.),
W A Johnson, and
N M Nathanson, and
A Horita
January 1986,
Brain research,
W A Johnson, and
N M Nathanson, and
A Horita
July 1987,
Endocrinology,
W A Johnson, and
N M Nathanson, and
A Horita
January 1987,
Peptides,
