-transparent.png){kind=logo}
Pyruvate dehydrogenase complex and lipoamide dehydrogenase were purified from muscle of Ascaris lumbricoides var. suum which contains relatively a large amount of the complex. Molecular weights of three constituent enzymes of Ascaris pyruvate dehydrogenase complex were as follows; alpha- and beta-subunits of pyruvate dehydrogenase were 42,000 and 37,000, respectively, lipoate acetyltransferase was 76,000 and lipoamide dehydrogenase was 56,000. Furthermore, two unknown polypeptides having molecular weight of 46,000 and 41,000 were detected. Anti-Ascaris lipoamide dehydrogenase antibody precipitated three constituent enzymes and two unknown polypeptides, suggesting that lipoamide dehydrogenase not only binds tightly to complex, but also two unknown polypeptides bind tightly to complex.
S Matuda, and
K Nakano, and
T Saheki
November 1979,
Biochimica et biophysica acta,
S Matuda, and
K Nakano, and
T Saheki
November 1986,
Molecular and biochemical parasitology,
S Matuda, and
K Nakano, and
T Saheki
April 1987,
Molecular and biochemical parasitology,
S Matuda, and
K Nakano, and
T Saheki
June 1983,
Molecular and biochemical parasitology,
S Matuda, and
K Nakano, and
T Saheki
January 1970,
Biokhimiia (Moscow, Russia),
S Matuda, and
K Nakano, and
T Saheki
January 1982,
Methods in enzymology,
S Matuda, and
K Nakano, and
T Saheki
July 1979,
Journal of biochemistry,
S Matuda, and
K Nakano, and
T Saheki
February 1981,
European journal of biochemistry,
S Matuda, and
K Nakano, and
T Saheki
May 1988,
Molecular and biochemical parasitology,
S Matuda, and
K Nakano, and
T Saheki
May 1998,
Archives of biochemistry and biophysics,
