- Abstract:
-
His-tagged cysteine-less F1Fo ATP synthase from Escherichia coli was purified using Ni-NTA affinity chromatography. During the purification procedure the loss of total ATPase activity did not exceed 50%, and the extent of purification was about 80-fold. The purified enzyme was essentially free of other proteins, was highly active in ATP hydrolysis (75 units/mg at pH 8 and 37 degrees C), and was sensitive to N,N'-dicyclohexylcarbodiimide (70%). Incorporation of F1Fo into soybean liposomes yiel...
Expand abstract - Publisher copy:
- 10.1016/j.bbabio.2004.09.012
-
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- Journal:
- Biochimica et biophysica acta
- Volume:
- 1706
- Issue:
- 1-2
- Pages:
- 110-116
- Publication date:
- 2005-01-05
- DOI:
- ISSN:
-
0006-3002
- URN:
-
uuid:edb7e656-7c6c-4cbe-9dd3-b038e95c0200
- Source identifiers:
-
159750
- Local pid:
- pubs:159750
- Copyright date:
- 2005
Journal article
Ultrafast purification and reconstitution of His-tagged cysteine-less Escherichia coli F1Fo ATP synthase.
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