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. 2015 May 26;10(5):e0127911. doi: 10.1371/journal.pone.0127911

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© 2015 Panicker et al

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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Fig 1 — (A) Proteins of the pTGP3 transformant were separated into hydrophobic and aqueous fractions by Triton X-114 partitioning. Equivalent amounts of the fractions were separated by SDS-PAGE in 10% polyacrylamide gels, Western transferred and probed with a monoclonal antibody against alkaline phosphatase. Lanes: W, whole cells; H, hydrophobic fraction; A, aqueous fraction. The molecular weight (MW) markers were the biotinylated protein ladder from Cell Signaling Technology. (B) The membrane and cytosolic fractions of transformant pTGP3 were separated by SDS-PAGE in a 10% polyacrylamide gel and Western transferred. Immunostaining with a monoclonal antibody to alkaline phosphatase demonstrated the presence of PhoA in the whole cells (lane W) and the membrane fraction (lane M), but not in the cytosolic fraction (lane C). (C) Whole cells of the pTGP3 transformant were treated with increasing concentrations of trypsin. The cells in lane 0 were treated with TS buffer only. Proteins were separated by SDS-PAGE in 10% polyacrylamide gels and immunostained with a monoclonal antibody against alkaline phosphatase.