Target Molecular Size of the Red Beet Plasma Membrane ATPase
Author(s) -
Donald P. Briskin,
W. R. Thornley,
Joseph L. Roti-Roti
Publication year - 1985
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.78.3.642
Subject(s) - vanadate , atpase , membrane , protein subunit , chemistry , enzyme , dimer , biochemistry , gel electrophoresis , biophysics , biology , gene , organic chemistry
Radiation inactivation of the red beet (Beta vulgaris L.) plasma membrane ATPase was carried out using gamma-ray radiation from a (137)Cs source. Inactivation of vanadate-sensitive ATPase activity by gamma-ray radiation followed an exponential decline with increasing total dose, indicating a single target size calculated to have a molecular weight of about 228,000. Since the catalytic subunit of the red beet plasma membrane ATPase has been demonstrated to have a molecular weight of about 100,000 by dodecyl-sulfate gel electrophoresis following (32)P-phosphorylation, it is suggested that the native enzyme may exist, at least, as a dimer of catalytic subunits.
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