-transparent.png){kind=logo}
Complex II (succinate-coenzyme Q reductase) was resolved into ten different polypeptides by polyacrylamide gel electrophoresis. Four polypeptides, CII-1, CII-2, CII-3, and CII-4 with molecular weights of 70 000, 24 000, 13 500, and 7000, were present in large amounts in all preparations examined. CII-1 and CII-2 are the flavoprotein and iron-sulfur protein, respectively, of succinate dehydrogenase; CII-3 and CII-4 have not been functionally indentified. Six polypeptides were present in much smaller amoumts as judged by staining intensity, and each of these comigrated with components in complex III. The amino acid compositions of several of the minor components in complex II were identical with that of an equivalently migrating polypeptide in complex III. We conclude that succinate-coenzyme Q reductase contains four different polypeptides and is contaminated with variable amounts of complex III when isolated as complex II.
R A Capaldi, and
J Sweetland, and
A Merli
October 1977,
Chemical & pharmaceutical bulletin,
R A Capaldi, and
J Sweetland, and
A Merli
February 1965,
Proceedings of the National Academy of Sciences of the United States of America,
R A Capaldi, and
J Sweetland, and
A Merli
July 2014,
Molecular syndromology,
R A Capaldi, and
J Sweetland, and
A Merli
February 1966,
Nature,
R A Capaldi, and
J Sweetland, and
A Merli
May 1967,
Biochemical and biophysical research communications,
R A Capaldi, and
J Sweetland, and
A Merli
December 1986,
Biokhimiia (Moscow, Russia),
R A Capaldi, and
J Sweetland, and
A Merli
August 1963,
Biochimica et biophysica acta,
R A Capaldi, and
J Sweetland, and
A Merli
May 1964,
Science (New York, N.Y.),
R A Capaldi, and
J Sweetland, and
A Merli
October 1969,
The Journal of biological chemistry,
R A Capaldi, and
J Sweetland, and
A Merli
December 1977,
Biochemical and biophysical research communications,
