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
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.
protein bodies
Prolamins
Somatotypes
Endosperm
Density Gradient Centrifugation
Pepsin A
Polyacrylamide Gel Electrophoresis
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.
In: Plant and Cell Physiology, Vol. 28, No. 8, 01.12.1987, p. 1517-1527.
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, vol. 28, no. 8, pp. 1517-1527.
Ogawa M, Kumamaru T, Satoh H, Iwata N, Omura T, Kasai Z et al. Purification of protein body-I of rice seed and its polypeptide composition. Plant and Cell Physiology. 1987 Dec 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. In: Plant and Cell Physiology. 1987 ; Vol. 28, No. 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",
journal = "Plant and Cell Physiology",
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
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.
JO - Plant and Cell Physiology
JF - Plant and Cell Physiology