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- W2011191723 abstract "F1-ATPase was isolated from yeast S.cerevisiae. The constituent subunits 1 and 2 were purified by gel permeation chromatography, and their amino acid compositions determined. Both subunits have a similar composition except for 12 cystine, methionine, leucine, histidine, and tryptophan. When F1 is treated for three hours with 5′-p-[3H]fluorosulfonylbenzoyl adenosine in dimethylsulfoxide, 90% of the activity is lost. Disc gel electrophoresis of the modified complex showed that over 90% of the label was associated with subunit 2. A labelled peptide from a S.aureus digest of subunit 2 was isolated and sequenced. It had the following amino acid sequence: His-Try∗-Asp-Val-Ala-Ser-Lys-Val-Gln-Glu, whereby Tyr∗ is the modified amino acid residue. This sequence shows homology to other sequences obtained from maize, beef heart, and E.coli F1-ATPases." @default.
- W2011191723 created "2016-06-24" @default.
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- W2011191723 date "1982-11-01" @default.
- W2011191723 modified "2023-10-16" @default.
- W2011191723 title "Modification of F1-ATPase from yeast Saccharomyces cerevisiae with 5′-p-[3H]fluorosulfonylbenzoyl adenosine" @default.
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- W2011191723 doi "https://doi.org/10.1016/0006-291x(82)91561-3" @default.
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