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Proteolysis of the delta subunit is required for release of the Ca2+, Mg2+-activated ATPase from the cell membrane of Escherichia coli

✍ Scribed by P.D. Bragg; C. Hou

Book ID
115910386
Publisher
Elsevier Science
Year
1979
Tongue
English
Weight
821 KB
Volume
103
Category
Article
ISSN
0014-5793

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## Abstract Crosslinking of membrane proteins of Escherichia coli with dithiobis (succinimidyl propionate) (DSP) resulted in loss of several enzyme activities including the Ca^2+^, Mg^2+^‐activated ATPase. This enzyme was crosslinked by DSP to the membrane and was not released by dialysis at low io

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We have partially purified active delta and epsilon subunits of the E. coli membranebound MgZf-ATPase (ECF1). Treating purified ECFl with 50% pyridine precipitates the major subunits (a, 0, and y ) of the enzyme, but the two minor subunits (6 and E ) , which are present in relatively small amounts,