Subunit tomato fruit

The psubunit has been purified from PGl by ourselves and others and is a heat stable, acidic, heavily glycosylated protein with an apparent molecular mass of 37-39 kD (19, 26). No enzymatic activity has been identified for the protein. The psubunit can be extracted from the cell walls of both green and ripe tomato fruit by high salt buffers (13, 14, 18, 19, 20), and in the latter case is associated with PG2 polypeptide(s) in the form of PGl. Purified psubunit can also associate with and convert PG2 in vitro into an isoenzyme that closely resembles PGl (13, 14, 24). Biochemical studies have shown that in vivo and in vitro formation of PGl by the association of PG2 with the p-subunit alters the biochemical and enzymic properties of the associated catalytic PG2 polypeptide including its pH optima, response to cations and thermal stability (summarized in Table 1). This later property provides a convenient assay for the levels of PGl and PG2 in total cell wall protein extracts. 

We propose that the tomato fruit B subunit is the archetypal member of a new class of plant cell wall proteins, which we have named AroGPs, for Aromatic Amino Acid Rich GlycoProteins. AroGPs have the following characteristics ... 

Enterotoxigenic E. coli B subunits of the heat labile toxin (LTB) Tomato fruit and leaf Offspring were passively immunized through oral immunization of parents. 91... 

E. coli B subunit of the heat labile enterotoxin (LTB) fused to an immu-nocontraceptive epitope Tomato fruit and leaves No immunogenicity assays performed. 91... 

B subunits of the cholera toxin (CTB) Tomato leaf and fruit No immunogenicity assays performed. — 120... 

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