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- W2026062525 abstract "Abstract— Purification of choline acetyltransferase (ChAc) from heads of Drosophila melanogaster , the richest known source of ChAc, has been accomplished. The stability of the enzyme was preserved by working with a concentration of protein above 0.1 mg/ml. The purification was carried out with ammonium sulfate fractionation and column chromatography on QAE‐Sephadex, CoA‐Sepharose, G‐200 Sephadex, and PCMB‐Sepharose. In a procedure using 100 g of Drosophila heads, the specific activity of the crude homogenate was 0.028 μmol/min/mg protein and that of the final product was 43 μmol/min/mg protein, representing a 1500 fold purification. A single protein band, containing all of the ChAc activity, was seen by polyacrylamide gel electrophoresis. A sharp pH optimum at 7.2 was observed. Apparent K m 's for acetyl CoA and choline were 90 μM and 47 μM , respectively. The molecular weight was determined to be 69,000. Isoelectric focusing of extracts of Drosophila heads showed only one peak of choline acetyltransferase activity with an apparent pi of 5.1." @default.
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- W2026062525 date "1978-05-01" @default.
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- W2026062525 title "PURIFICATION OF CHOLINE ACETYLTRANSFERASE FROM DROSOPHILA MELANOGASTER" @default.
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- W2026062525 doi "https://doi.org/10.1111/j.1471-4159.1978.tb12408.x" @default.
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