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An angiotensin II-binding activity has been detected in the 100,000 x g supernatant fraction of rabbit liver. The total amount of binding activity in this fraction was substantially greater than that which could be solubilized from hepatic particles by treatment with digitonin. The crude soluble binding activity resembled the binding protein which had been purified from the particles in several respects. First, binding required the presence of p-chloromercuriphenylsulfonic acid and bound angiotensin II was released by dithiothreitol. Second, the molecular weight of the responsible protein cross-linked to radioiodinated angiotensin II was about 75,000 in the reduced, denatured state. Finally, guinea pig antiserum raised against the binding protein that had been purified from particles reacted identically with the soluble and solubilized activities.
E Rosenberg, and
M A Ravi Kiron, and
R L Soffer
March 1989,
The Journal of biological chemistry,
E Rosenberg, and
M A Ravi Kiron, and
R L Soffer
March 1984,
Proceedings of the National Academy of Sciences of the United States of America,
E Rosenberg, and
M A Ravi Kiron, and
R L Soffer
October 1983,
European journal of biochemistry,
E Rosenberg, and
M A Ravi Kiron, and
R L Soffer
May 1976,
Biochemical pharmacology,
E Rosenberg, and
M A Ravi Kiron, and
R L Soffer
May 1974,
The Journal of infectious diseases,
E Rosenberg, and
M A Ravi Kiron, and
R L Soffer
August 1986,
The Biochemical journal,
E Rosenberg, and
M A Ravi Kiron, and
R L Soffer
September 1992,
The Journal of biological chemistry,
E Rosenberg, and
M A Ravi Kiron, and
R L Soffer
September 1962,
Biochimica et biophysica acta,
E Rosenberg, and
M A Ravi Kiron, and
R L Soffer
June 1968,
Biochimica et biophysica acta,
E Rosenberg, and
M A Ravi Kiron, and
R L Soffer
February 1971,
Biochemical and biophysical research communications,
