Purification and complete amino acid sequence of a major prolamin of rice endosperm

Horikoshi, Masako; Kobayashi, H.; Yamazoe, Yasushi; Mikami, Bunzo; Morita, Yukari

doi:10.1016/s0733-5210(09)80013-1

Cited by 10 publications

(8 citation statements)

References 22 publications

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“…The contribution of these non-polar amino acids (55 to 58 percent) made the protein more hydrophobic. Similar results were reported by Horikoshi et al [21] for the Amino acid residues were calculated by taking into account of mole % and the molecular weight of protein calculated from SDS-PAGE (Esen et al, 1985).…”

Section: Sds-page and Rp-hplcsupporting

confidence: 81%

“…In contrast, prolamins from barnyard and little millets showed cross reactivity with the polypeptide in the 20 kD region and the lower molecular weight polypeptides. The cross reactivity among prolamin polypeptides can be explained as they may be encoded by multigene families [21]. Recently, Esen [11] used monoclonal antibodies to four alphazein components to show structural similarities among the individual alphazein polypeptides.…”

Section: Sds-page and Rp-hplcmentioning

confidence: 99%

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Isolation and characterization of a 20 kD prolamin from kodo millet (Paspalum scrobiculatum) (L.): Homology with other millets and cereals

Parameswaran

Thayumanavan

1997

Plant Food Hum Nutr

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The homologus 20 kD prolamin from kodo millet and other minor millets viz. barnyard, little and foxtail millets, were purified using preparative gel electrophoresis and reversed phase high performance liquid chromatography (RP-HPLC). The amino acid composition of the purified 20 kD prolamin protein from different minor millets revealed higher content of glutamic acid, alanine, leucine and serine and lower quantity of lysine and methionine. They contain 55 to 58 percent of non-polar amino acids which make them more hydrophobic than other protein fractions. The total number of amino acid residues per polypeptide chain ranged from 152 to 155 based on theoretical calculation. Peptide mapping of the 20 kD prolamin hydrolyzed with trypsin gave fewer cleavage products than expected. The antigenic relationships among these minor millets and cereals viz. wheat, maize, rice, sorghum, finger millet and pearl millet were studied using the antibody raised against the 20 kD prolamin. Cross reactivity was seen in all the minor millets at the 20 kD region. But in barnyard and little millets lower molecular weight polypeptides also cross reacted with the antibody. Immunoblotting studies revealed that the prolamins from other cereals and millets are related to the 20 kD prolamin of kodo millet. Rice was the only common cereal that did not cross react immunologically with the antibody raised against 20 kD prolamin of kodo millet.

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Section: Sds-page and Rp-hplcsupporting

confidence: 81%

Section: Sds-page and Rp-hplcmentioning

confidence: 99%

Isolation and characterization of a 20 kD prolamin from kodo millet (Paspalum scrobiculatum) (L.): Homology with other millets and cereals

Parameswaran

Thayumanavan

1997

Plant Food Hum Nutr

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“…The prolamin fraction contained glutamate plus glutamane, alanine and leucine at high levels, but lysine and sulfur amino acids at low levels. The glutelin fraction was also characteristic of rice in this respect as described previously (6,23,24,26). As a matter of course, there was no difference in amino acid composi tion between Kuromai and Akamai rice lines.…”

Section: Methodssupporting

confidence: 72%

Efficient Extraction and Some Properties of Storage Proteins (Prolamin and Glutelin) in Ancient Rice Cultivars.

Udaka

Koga

Tsuji³

et al. 2000

Journal of Nutritional Science and Vitaminology, J Nutr Sci Vit

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“…Prolamins are encoded by a multigene family, and separated into three major groups according to their apparent molecular sizes of 10, 13, and 16 kDa ( Ogawa et al , 1987 ). The 13 kDa prolamins are the most abundant group of prolamins in rice ( Horikoshi et al , 1991 ). A chimeric gene encoding a fusion protein of 13 kDa prolamin (λRM1) and GFP was constructed.…”

Section: Resultsmentioning

confidence: 99%

A green fluorescent protein fused to rice prolamin forms protein body-like structures in transgenic rice

Saito

Kishida

Takata

et al. 2009

Journal of Experimental Botany

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Prolamins, a group of rice (Oryza sativa) seed storage proteins, are synthesized on the rough endoplasmic reticulum (ER) and deposited in ER-derived type I protein bodies (PB-Is) in rice endosperm cells. The accumulation mechanism of prolamins, which do not possess the well-known ER retention signal, remains unclear. In order to elucidate whether the accumulation of prolamin in the ER requires seed-specific factors, the subcellular localization of the constitutively expressed green fluorescent protein fused to prolamin (prolamin–GFP) was examined in seeds, leaves, and roots of transgenic rice plants. The prolamin–GFP fusion proteins accumulated not only in the seeds but also in the leaves and roots. Microscopic observation of GFP fluorescence and immunocytochemical analysis revealed that prolamin–GFP fusion proteins specifically accumulated in PB-Is in the endosperm, whereas they were deposited in the electron-dense structures in the leaves and roots. The ER chaperone BiP was detected in the structures in the leaves and roots. The results show that the aggregation of prolamin–GFP fusion proteins does not depend on the tissues, suggesting that the prolamin–GFP fusion proteins accumulate in the ER by forming into aggregates. The findings bear out the importance of the assembly of prolamin molecules and the interaction of prolamin with BiP in the formation of ER-derived PBs.

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Purification and complete amino acid sequence of a major prolamin of rice endosperm

Cited by 10 publications

References 22 publications

Isolation and characterization of a 20 kD prolamin from kodo millet (Paspalum scrobiculatum) (L.): Homology with other millets and cereals

Isolation and characterization of a 20 kD prolamin from kodo millet (Paspalum scrobiculatum) (L.): Homology with other millets and cereals

Efficient Extraction and Some Properties of Storage Proteins (Prolamin and Glutelin) in Ancient Rice Cultivars.

A green fluorescent protein fused to rice prolamin forms protein body-like structures in transgenic rice

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