AI Article Synopsis
- The genes of two closely related phospholipase D isoenzymes (PLD1 and PLD2) from white cabbage have been sequenced and expressed in E. coli.
- Both enzymes are highly similar, showing 91% identity and comparable behavior in various analyses.
- Phospholipase D purified from cabbage leaves (PLDcab) is identified as corresponding to PLD2, but it differs by being N-terminally acetylated unlike the recombinant version.
Article Abstract
Recently, the genes of two isoenzymes of phospholipase D from white cabbage (PLD1 and PLD2) with molecular masses of 91.7 and 91.9 kDa, respectively, have been sequenced and expressed in Escherichia coli [Schäffner, I., Rücknagel, K.-P., Mansfeld, J., and Ulbrich-Hofmann, R. (2002). Eur. J. Lipid Sci. Technol. 104: 79-87]. Both enzymes are highly homologous (91% identity) and behave very similarly. Phospholipase D purified from white cabbage leaves (PLDcab) is compared with the two recombinant enzymes in sodium dodecylsulfate and native polyacrylamide gel electrophoresis, isoelectric focusing, N-terminal sequencing, and mass spectrometry after tryptic digestion. As a result, PLDcab clearly can be assigned to PLD2. In contrast to recombinant PLD2, however, PLDcab is N-terminally acetylated.
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| http://dx.doi.org/10.1023/a:1021182500299 | DOI Listing |
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