Purification of protein body-I of rice seed and its polypeptide composition

Masahiro Ogawa, Toshihiro Kumamaru, Hikaru Satoh, Nobuo Iwata, Takeshi Omura, Zenzaburo Kasai, Kunisuke Tanaka

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Abstract

Protein body type one (PB-I) was isolated and purified from developing rice grain by a combination of sucrose density gradient centrifugation and treatment with pepsin. SDS-PAGE analysis showed that isolated PB-I contains several polypeptide groups, the largest having an apparent molecular size of 13 kDa and two smaller ones of 10 kDa and 16 kDa. The 13-kDa group was found to be composed of two polypeptides of slightly different molecular sizes, 13a (larger component) and 13b (smaller component). Most of the 13a and 13b polypeptides were shown to be largely prolamins, although there were also some salt- and alcohol-insoluble polypeptides with an apparent molecular size of 13 kDa. It was concluded that PB-I is the accumulation site of rice prolamin. It was further estimated that the protein amount in PB-I accounted for about 20% of the total protein of rice endosperm.

Original languageEnglish
Pages (from-to)1517-1527
Number of pages11
JournalPlant and Cell Physiology
Volume28
Issue number8
Publication statusPublished - Dec 1 1987

All Science Journal Classification (ASJC) codes

  • Physiology
  • Plant Science
  • Cell Biology

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    Ogawa, M., Kumamaru, T., Satoh, H., Iwata, N., Omura, T., Kasai, Z., & Tanaka, K. (1987). Purification of protein body-I of rice seed and its polypeptide composition. Plant and Cell Physiology, 28(8), 1517-1527.