A Cross-Linking Study of the Ca2+, Mg2+-Activated Adenosine Triphosphatase of Escherichia coli
✍ Scribed by Philip D. BRAGG; Cynthia HOU
- Book ID
- 115118766
- Publisher
- John Wiley and Sons
- Year
- 1980
- Tongue
- English
- Weight
- 841 KB
- Volume
- 106
- Category
- Article
- ISSN
- 1432-1327
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## Abstract Previous studies have shown that mutations in the __unc__ gene of __Escherichia coli__ K12 cause defects in energy transduction as well as in a membrane‐bound (Mg^2+^,Ca^2+^)· adenosine triphosphatase. We studied the effect of this mutation on the “downhill” efflux of methyl‐β‐D‐galact
## 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