Abstract
A glycoprotein with an apparent molecular mass of 42 kDa (GP42), detected in the roots of Lupinus albus L. (cv. Rio Maior), was found to increase along the root axis with increasing distance from the apex and to be induced in roots cultured in vitro upon exogenous supply of high IAA (10‐3M). GP42 is ionically bound to the cell wall, it has a pl>8.3, and it is N‐glycosylated. The purification of GP42 was accomplished by affinity chromatography (ConA‐Sepharose) followed by cation‐exchange chromatography (Mono S). The amino acid sequence of the amino terminal part of the protein shows 70% identity to that of polygalacturonase inhibitor proteins (PGIPs) from other species. GP42 inhibits the polygalacturonase activity from Aspergilltus niger in vitro suggesting that it is a PGIP. The possible relationship between the L. albus PGIP and root development is discussed.
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