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

研究成果: ジャーナルへの寄稿記事

158 引用 (Scopus)

抄録

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.

元の言語英語
ページ(範囲)1517-1527
ページ数11
ジャーナルPlant and Cell Physiology
28
発行部数8
出版物ステータス出版済み - 12 1 1987

Fingerprint

protein bodies
polypeptides
Seeds
Prolamins
rice
Peptides
prolamins
seeds
Proteins
Somatotypes
rice protein
Endosperm
Density Gradient Centrifugation
Pepsin A
pepsin
endosperm
Sucrose
Polyacrylamide Gel Electrophoresis
alcohols
Salts

All Science Journal Classification (ASJC) codes

  • Physiology
  • Plant Science
  • Cell Biology

これを引用

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.

Purification of protein body-I of rice seed and its polypeptide composition. / Ogawa, Masahiro; Kumamaru, Toshihiro; Satoh, Hikaru; Iwata, Nobuo; Omura, Takeshi; Kasai, Zenzaburo; Tanaka, Kunisuke.

:: Plant and Cell Physiology, 巻 28, 番号 8, 01.12.1987, p. 1517-1527.

研究成果: ジャーナルへの寄稿記事

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, 巻. 28, 番号 8, pp. 1517-1527.
Ogawa M, Kumamaru T, Satoh H, Iwata N, Omura T, Kasai Z その他. Purification of protein body-I of rice seed and its polypeptide composition. Plant and Cell Physiology. 1987 12 1;28(8):1517-1527.
Ogawa, Masahiro ; Kumamaru, Toshihiro ; Satoh, Hikaru ; Iwata, Nobuo ; Omura, Takeshi ; Kasai, Zenzaburo ; Tanaka, Kunisuke. / Purification of protein body-I of rice seed and its polypeptide composition. :: Plant and Cell Physiology. 1987 ; 巻 28, 番号 8. pp. 1517-1527.
@article{ebb366ba167341b680de0b19c7db683b,
title = "Purification of protein body-I of rice seed and its polypeptide composition",
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.",
author = "Masahiro Ogawa and Toshihiro Kumamaru and Hikaru Satoh and Nobuo Iwata and Takeshi Omura and Zenzaburo Kasai and Kunisuke Tanaka",
year = "1987",
month = "12",
day = "1",
language = "English",
volume = "28",
pages = "1517--1527",
journal = "Plant and Cell Physiology",
issn = "0032-0781",
publisher = "Oxford University Press",
number = "8",

}

TY - JOUR

T1 - Purification of protein body-I of rice seed and its polypeptide composition

AU - Ogawa, Masahiro

AU - Kumamaru, Toshihiro

AU - Satoh, Hikaru

AU - Iwata, Nobuo

AU - Omura, Takeshi

AU - Kasai, Zenzaburo

AU - Tanaka, Kunisuke

PY - 1987/12/1

Y1 - 1987/12/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0000787179&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0000787179&partnerID=8YFLogxK

M3 - Article

VL - 28

SP - 1517

EP - 1527

JO - Plant and Cell Physiology

JF - Plant and Cell Physiology

SN - 0032-0781

IS - 8

ER -