Abstract：
:(Na+ + K+)ATPase contains two different subunits, a catalytic subunit (alpha) and a subunit with uncertain function (beta). The enzyme binds ATP, ouabain and vanadate, and can be phosphorylated by ATP as well as by inorganic phosphate. From the previously reported maximal binding and phosphorylation capacities of 3.5--4.3 nmol P per mg protein (based on Lowry protein determination) and the earlier molecular weight value of approximately 250,000, a molar binding and phosphorylation capacity of 0.87--1.07 mol per mol enzyme was derived. As it is generally agreed that the enzyme molecule contains two alpha subunits or even a multiple of two, it has been suggested that the enzyme operates by means of a so-called "half-of-the-sites mechanism" whereby only of the two alpha subunits can be phosphorylated at any one time. We now present evidence that every alpha subunit can be phosphorylated simultaneously, which rules out the operation of such a mechanism.
journal_name
Naturejournal_title
Natureauthors
Peters WH,Swarts HG,de Pont JJ,Schuurmans Stekhoven FM,Bonting SLdoi
10.1038/290338a0subject
Has Abstractpub_date
1981-03-26 00:00:00pages
338-9issue
5804eissn
0028-0836issn
1476-4687journal_volume
290pub_type
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