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PLANT PHYSIOLOGY , Vol 110, Issue 3 875-882, Copyright © 1996 by American Society of Plant Biologists

BIOCHEMISTRY AND ENZYMOLOGY

Isolation and Identification of Ripening-Related Tomato Fruit Carboxypeptidase

R. A. Mehta and A. K. Mattoo
Plant Molecular Biology Laboratory, Beltsville Agricultural Research Center, United States Department of Agriculture/Agricultural Research Service, Beltsville, Maryland 20705-2350 (R.A.M., A.K.M.)

Tomato (Lycopersicon esculentum) fruit carboxypeptidase active on N-carbobenzoxy Z-L-phenylalanine-L-alanine was found to constitute a family of isoforms whose abundance changed differentially during ripening. A specific polyclonal antibody against the fruit carboxypeptidase was raised in rabbits and used to purify and identify the protein. The data from immunoaffinity chromatography, immunoinhibition studies, immunoprecipitation of the in vivo- and in vitro-labeled proteins, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of native isoforms strongly suggest that the fruit carboxypeptidases are monomers or oligomers of 68- and/or 43-kD subunits.


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