Plasma Membrane ATPase of Red Beet Forms a Phosphorylated Intermediate
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چکیده
منابع مشابه
Plasma membrane ATPase of red beet forms a phosphorylated intermediate.
When a plasma membrane-enriched fraction isolated from red beet (Beta vulgaris L.) was incubated in the presence of 40 micromolar [gamma-(32)P] ATP, 40 micromolar MgSO(4) at pH 6.5, a rapidly turning over phosphorylated protein was formed. Phosphorylation of the protein was substrate-specific for ATP, sensitive to diethylstilbestrol and vanadate, but insensitive to azide. When the dephosphoryla...
متن کاملThe purified plasma membrane ATPase of the yeast Schizosaccharomyces pombe forms a phosphorylated intermediate.
An acid slab gel electrophoresis method of high-resolving power allows detection of a phosphorylated form in the purified ATPase of the yeast Schizosaccharomyces pombe and identification of this catalytic intermediate among the different phosphopeptides of a plasma membrane preparation. At a maximum steady state rate of MgATP hydrolysis by the membrane-bound ATPase, 20 to 40% of the ATPase subu...
متن کاملCharacterization of the solubilized plasma membrane ATPase of red beet.
The plasma membrane ATP-phosphohydrolase (ATPase) from red beet (Beta vulgaris L.) storage tissue was solubilized with the zwitterionic detergent Zwittergent 3-14 from a plasma membrane-enriched fraction which was extracted with the anionic detergent, sodium deoxycholate. For both the extraction of extraneous proteins by deoxycholate and the solubilization of active plasma membrane ATPase by Zw...
متن کاملTarget molecular size of the red beet plasma membrane ATPase.
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 o...
متن کاملEvidence for a /B-Aspartyl Phosphate Residue in the Phosphorylated Intermediate of the Red Beet Plasma Membrane
A borohydride reduction method was used to identify the phosphorylated amino acid in the phospho-enzyme of the red beet (Beta vulgani L.) plasma membrane ATPase. Plasma membrane fractions were phosphorylated with unlabeled ATP in the presence of MgSO4 at pH 6.5 and then treated with sodium l3Hlborohydride. The borohydride-treated samples were subjected to hydrolysis in 6 normal HCI at 110°C for...
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ژورنال
عنوان ژورنال: Plant Physiology
سال: 1983
ISSN: 0032-0889,1532-2548
DOI: 10.1104/pp.71.3.507