Electrophoretic variation of Lectin-like proteins was investigated in wild and cultivated common bean accessions. In three seeds, all from Mexico, LLP polypeptides were not detectable. In a fouth seed, two abundant glycoplypeptides with Mr of about 32-35 kDa, were present. The Mr suggests that LLP is not proteolitically cleaved in the protein bodies and accumulates in a form similar to that of newly-synthesized LLp precursors transiently associated to the ER.
Electrophoretic variation in a "lectin-like" protein of bean seeds
Bollini R;Daminati MG;Lioi L;Vitale A;Ceriotti A
1989
Abstract
Electrophoretic variation of Lectin-like proteins was investigated in wild and cultivated common bean accessions. In three seeds, all from Mexico, LLP polypeptides were not detectable. In a fouth seed, two abundant glycoplypeptides with Mr of about 32-35 kDa, were present. The Mr suggests that LLP is not proteolitically cleaved in the protein bodies and accumulates in a form similar to that of newly-synthesized LLp precursors transiently associated to the ER.File in questo prodotto:
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