Polygalacturonase inhibitors in bean pods.
The amount of polygalacturonase-inhibiting protein (PGIP) was 14 times higher in bean pods than in etiolated hypocotyls. The PGIP was extracted from bean pods and partially purified by chromatography on columns of S-Sepharose. DEAE-Sephadex A-50, and Sephadex G-75. Further purification by ion-exchange chromatography on a Mono Q column separated two isoforms of the inhibitor. The two PGIPs were similar in most properties but differed slightly in pI values. They also differed in one residue of the N-terminal amino acid sequences. Both bean pod PGIPs differed in two and possibly three residues of the deduced N-terminal amino acid sequence for hypocotyl PGIP. Small alterations in the structure of PGIP may represent a strategy in bean plants for resistance to a variety of pathogens.
Pressey
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USDA, ARS, Richard B. Russell Research Center, Athens, GA 30604-5677, USA.
D000595:Amino Acid Sequence; D002852:Chromatography, Ion Exchange; D007887:Fabaceae / Q000737:chemistry*; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification*; D010946:Plants, Medicinal; D011096:Polygalacturonase / Q000037:antagonists & inhibitors*
C081479:PGIP protein, plant; D010940:Plant Proteins; D011096:Polygalacturonase