抄録
Study of the soluble proteins of sweet potato (Ipomoea batatas L. cv. Norin 1) roots showed that the major protein had an apparent molecular weight of 25, 000, and accounted for 60-70% of the total soluble protein extracted from fresh tissue. The 25-kDa protein exists in two forms, which can be resolved into two bands by nondenaturing polyacrylamide gel electrophoresis. Immunodiffusion and crossed immunoelectrophoresis showed that these forms are immunologically identical. This protein was identified as the antigenic component A of sweet potato root.1) It was degraded to proteins of lower molecular weight (9, 500 to 20, 000) if the tissue was cut or infected by Ceratocystis fimbriata. As almost none of this 25-kDa protein was detected in roots stored for one year at 10-12°C, it is probably the storage protein of these roots. Another major protein was identified as β-amylase by immunodiffusion and immunoelectrophoresis. The amount of β-amylase did not change appreciably after cutting or infection, but it was present in only trace amounts in the roots stored for one year, Cutting, infection, or storage of root tissue resulted in the production of new isozymes of peroxidase, acid phosphatase, and esterase. Increases in some other proteins in cut and in diseased tissues were detected by gel electrophoresis.
