TY - JOUR
T1 - Adenosine triphosphatase from rat liver mitochondria. III. Subunit composition
AU - Catterall, W. A.
AU - Coty, W. A.
AU - Pedersen, P. L.
N1 - Copyright:
Copyright 2004 Elsevier B.V., All rights reserved.
PY - 1973
Y1 - 1973
N2 - Preparations of mitochondrial ATPase from rat liver mitochondria contain five classes of polypeptide chains. Consistent with previous results, the three major classes of polypeptide chains, designated subunits A,B, and C, have apparent molecular weights of 62,500, 57,000, and 36,000, respectively, as determined by gel electrophoresis in sodium dodecyl sulfate. These subunits have been isolated in purified form. They comprise approximately 97% of the mass of the enzyme preparation and are present in the enzyme complex in the stoichiometry A3B3C. The two minor classes of polypeptide chains have molecular weights of 12,500 and approximately 7,500 as determined by gel electrophoresis in sodium dodecyl sulfate. They appear to comprise less than 3% of the mass of the enzyme preparation.
AB - Preparations of mitochondrial ATPase from rat liver mitochondria contain five classes of polypeptide chains. Consistent with previous results, the three major classes of polypeptide chains, designated subunits A,B, and C, have apparent molecular weights of 62,500, 57,000, and 36,000, respectively, as determined by gel electrophoresis in sodium dodecyl sulfate. These subunits have been isolated in purified form. They comprise approximately 97% of the mass of the enzyme preparation and are present in the enzyme complex in the stoichiometry A3B3C. The two minor classes of polypeptide chains have molecular weights of 12,500 and approximately 7,500 as determined by gel electrophoresis in sodium dodecyl sulfate. They appear to comprise less than 3% of the mass of the enzyme preparation.
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M3 - Article
C2 - 4126855
AN - SCOPUS:0015889686
SN - 0021-9258
VL - 248
SP - 7427
EP - 7431
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 21
ER -