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- W2361497165 abstract "In order to reveal the mechanism of wheat polygalacturonase-inhibiting protein (PGIP) and to make best use of it in gene engineering, its structure was studied. The N-terminal amino acid sequence of wheat PGIP was determined by Edman degradation. The result was: Lys-Pro-Leu-Leu-Thr-Lys-Ile-Thr-Lys-Gly-Ala-Ala-Ser-Thr. The secondary structure of wheat PGIP was obtained by the measurement of circular dichroic spectra. The native PGIP of wheat was estimated to contain about 43.7% β-sheet and 13.1% α-helix. The secondary structure was changed by effects of pH and temperature. α-helix had little change and β-sheet was destroyed while the protein denatured incompletely. When the activity of wheat PGIP lost, the content of β-sheet varied a little and that ofα-helix reduced apparently. Wheat PGIP had internal disulfide bond by analysis of NR/R (not reduced/reduced) two-dimensional electrophoresis. Wheat PGIP was deglycosylated using TFMS, and the result indicated that carbohydrates content was 22%. When dicotyledon PGIPs was compared with wheat PGIP, there was difference in primary structure. The N-terminal sequence of PGIPs in dicotyldonous plants shared 36% identical amino acids, but the percentage of overall identity was changed to only 9% when wheat PGIP was included in the analysis. However, PGIPs from Wheat and dicotyledon were consistent in secondary structure, disulfide bond and carbohydrates content. The results have laid the foundation for the elucidation of its mechanism, and is significant for breeding crops resistant to Gibberella zeae(Schw.) Petch." @default.
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- W2361497165 date "2002-01-01" @default.
- W2361497165 modified "2023-09-25" @default.
- W2361497165 title "The Partial Structure of Wheat Polygalacturonase-inhibiting Protein" @default.
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