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Localization of a protein a‐tagged kex2 protein to the vacuole of Saccharomyces cerevisiae allows rapid purification of vacuolar membranes
Author(s) -
Bryant Nia J.,
Boyd Alan
Publication year - 1995
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.320110302
Subject(s) - vacuole , biology , golgi apparatus , saccharomyces cerevisiae , membrane , lysis , organelle , yeast , protease , microbiology and biotechnology , tandem affinity purification , biochemistry , cell , cytoplasm , affinity chromatography , enzyme
We have previously reported an immunoisolation procedure which allows purification of Kex2p‐containing Golgi membranes from lysed yeast cells. In order to evaluate the use of tagging procedures in organelle isolation we set out to isolate the same Golgi membrane fraction using a version of the Kex2 protease that had been affinity‐tagged at its C‐terminus. This protein is found to be localized in the vacuole, providing the basis of a method for the affinity‐purification of vacuolar membranes.