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PLANT PHYSIOLOGY , Vol 109, Issue 3 743-750, Copyright © 1995 by American Society of Plant Biologists

BIOCHEMISTRY AND ENZYMOLOGY

Identification and Characterization of a Phloem-Specific [beta]-Amylase

Q. Wang, J. Monroe and R. D. Sjolund
Department of Biological Sciences, University of Iowa, Iowa City, Iowa 52242 (Q.W., R.D.S.)

A monoclonal antibody, RS 5, was raised by injecting sieve elements isolated from tissue cultures of Streptanthus tortuosus (Brassicaceae) into BALB/c mice and screening resultant hybridoma supernatants for the labeling of phloem using immunofluorescence microscopy. The RS 5 monoclonal antibody identifies a 57-kD protein on immunoblots, which is present in phloem-forming tissue cultures of S. tortuosus but is absent in cultures that lack phloem. Purified 57-kD protein of S. tortuosus is demonstrated to be a phloem-specific [beta]-amylase. Partial peptide sequences of the 57-kD protein of S. tortuosus are shown to be 96% identical with the corresponding portions of a deduced sequence reported for a major form of [beta]-amylase in Arabidopsis thaliana. The RS 5 antibody cross-reacts with the major form of A. thaliana [beta]-amylase on immunoblots, and the antibody also binds to the sieve elements of A. thaliana using immunofluorescence microscopy. The results suggest that the major form of A. thaliana [beta]-amylase is a phloem-specific enzyme.


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