Abstract
A unique esterase isozyme ‘z’ with very low electrophoretic mobility on the anionic polyacrylamide gel (PAGE) was found in the medium of a non-embryogenic (Ca-4) line of cultured carrot (Daucus carota L.) cells. The protein corresponding to this esterase isozyme ‘z’ was purified by electroelution from preparative PAGE and the esterase migrated as a single band with an apparent Mr of 35 000 on SDS-PAGE. The purified esterase isozyme ‘z’ exhibited at least 350-fold higher specific activity than that in the total medium proteins.
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