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Ultrafast purification and reconstitution of His-tagged cysteine-less Escherichia coli F1Fo ATP synthase.

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...

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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

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