• Applied Biological Chemistry
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• v.32 no.1
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• pp.64-72
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• 1989

Near full length cDNA clones encoding the rice seed storage protein, prolamine, were isolated and divided into two homology classes based on cross-hybridization and DNA sequencing analysis. These cDNA clones contain a single open reading frame encoding a putative rice prolamine precursor(M.W.=17,200) possessing atypical 14 amino acid signal peptide. Clones of these two homology classes diverge mainly by insertions/deletions of short nucleotide stretches and point mutations. The deduced primary structures of both types of prolamine polypeptides are devoid of any major tandem repetitive sequences, a feature prevalent in other cereal prolamines. No significant homology teas detected between the rice prolamine and other cereal prolamines, indicating that the rice gene evolved from a different ancestor that gave rise to other cereal prolamine genes. Developing wheat and rice endosperms were examined using ultrathin sections prepared from tissues harvested at various days after flowering. By immunocytochemical localization techniques, wheat prolamines are localized within vesicles from Golgi apparatus and in homogeneous regions of protein bodies. The involvement of the goli apparatus in the packaging of wheat prolamines into protein bodies indicates a pathway which differs from the mode of other cereal prolamines and resembles the mechanism employed for the storage of rice glutelin and legume globulins.

• Applied Biological Chemistry
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• v.36 no.6
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• pp.525-532
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• 1993

To characterize the prolamines in rice cultivars, the complete coding sequences of 17 prolamine genes from the database were analyzed. According to the phylogenic analysis of the sequences, these genes could be classified into 4 groups, Group I to IV. The multiple alignment of the deduced amino acid sequences revealed that the four groups differ from one another in chain length caused by deletion of short internal amino acids or carboxyl terminal fragments. Each group was also found to have different amino acid composition with 1, 4, 10 and 30% of sulfur containing amino acids (methionine and cysteine) in Group I to IV prolamines, respectively. Also the isoelectric points of these groups showed the different values of 9.2, 8.2, 6.7 and 7.4. Finally, from the analysis of codon usage pattern of prolamine genes, the codon usage for arginine, serine, threonine, isoleucine, asparagine, aspartic acid, glutamic acid and cysteine were higly biased. In the analysis of the codon usage pattern, the relation of the fraction of G/C ending codons to effective codon numbers suggests the different translational efficiency in the expression of the prolamine multigenes.

• Applied Biological Chemistry
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• v.10
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• pp.15-21
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• 1968

In order to fractionate the rice protein employing paper electrophoresis, 9 subjects of Korean rice and one Indica type, Pin Galw 50 were examined, the results were as follows. 1. Polished rice protein was separated into albumin, globulin, prolamine, and oryzenin. The amount of these fractions was determined by Kjeldahl method showing respectively 0.26%, 0.65%, 0.41%, and 5.01% in average. Albumin was extracted with deionized water, globulin with 10% NaCl, prolamine with 70% ethanol, and oryzenin with 0.05N-NaOH. 2. Albumin was extracted with deionized water and dialyzed by a cellophan tube. The supernatant was submitted to paper electrophoresis using phosphate buffer (pH 7.6, ${\mu}$ 0.18). Albumin was identified as monocomponent in all of 10 varieties under study. Globulin was extracted and dialyzed to remove the albumin. The precipitates were resolved in 10% saline solution and examined by paper electrophoresis. The globulin consists of two components in phosphate buffer(pH 7.6, ${\mu}$ 0.18) Any subject, regardless the origin, appears to contain globulin I and globulin II. Prolamine was extracted with 70% ethanol, dialayzed against deionized water, resolved with ethanol, and analyzed by Paper electrophoresis. It was proved as one component in the 70% alcoholic buffer(pH 9.0, ${\mu}$=0.0095). On the contrary, paper electrophoresis with oryzenin demonstrated two or three components in Sorensen's buffer(pH 13.0, ${\mu}$ 0.11). Yookoo 132, Dungpan 5, Kwansan, and Jaekun contain oryzenin I, oryzenin II, and oryzenin III. On the other hand, Paldal, Jinheung, Sukwang, Eunbangzu, Damakum, and Pin Galw 56 contain only oryzenin II, and oryzenin III. On the basis of these analyses a discussion of the differences between the protein fractions of 10 varieties was presented. 3. Globulin I varied from 0.22% to 0.46% (aver. 0.35%) in the amount, globulin II from 0.21 to 0.44%(aver. 0.32%), oryzenin I from 0.17% to 0.44%(aver. 0.3%), oryzenin II from 1.59% to 2.88%(aver. 2.23%), and oryzenin III from 2.02% to 3.57%(aver. 2.66%).

• Journal of Plant Biology
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• v.37 no.3
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• pp.293-299
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• 1994

Developing rice endosperm cells display two morphologically distinct rough endoplasmic reticulum (ER) membranes, the cisternae ER (C-ER) and theprotein body ER (PB-ER), the latter delimiting the prolamine protein bodies. We (Li et al., 1993) have recently shown that the storage protein mRNAs are not randomly distributed on these ER types; the C-ER is enriched for glutelin mRNAs, whereas the PB-ER harbors predominantly prolamine transcripts. To address whether these ER types have differnet capacities to translate these mRNAs and translocate their proteins into the lumen, a microsomal fraction enriched in C-ER vesicles was prepared from devleoping rice seeds. When present in an in vitro translatin system, the microsomes were able to proteolytically remove the signal peptide and internalize both preproglutelin and preprolamine within the microsomal vesicles. Of the two species, preprolamine was more effectively translocated and processed. These results suggest that the C-ER has the capacity to recognize and bind both storage protein mRNAs during protein synthesis. Moreover, efficient translocation and processing of glutelin requires additional factors that are deficient or absent in the in vitro system.

• Korean Journal of Food Science and Technology
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• v.17 no.5
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• pp.377-388
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• 1985

The changes in protein fractions and its gel electrophoretic pattern of rapeseeds (Brassica napus L) were investigated during germination at $25^{\circ}C$ under dark condition. The major protein fraction was found to be albumin 25.0%) and globulin (24.6%). Both fractions were decreased throughout germination, particularly significant for albumin, while prolamine(2.2%) and glutelin (1.8%) showed an initial decrease followed by a slow increase at the later stage of germination. The initial 5-6 peaks of gel electrophoresis were reduced to a few after 45 hours. The absorption spectrum at the range of 400-700 nm showed a significant increase in absorbance for sodium hexametaphosphate (SHMP) extract of rapeseeds. The protein extractability with SHMP was not significantly affected by germination.

• Applied Biological Chemistry
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• v.12
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• pp.13-17
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• 1969

The fractions of protein, albumin, globulin, oryzenin, and prolamine extracted from 20 varieties of rice were determined, which include upland and paddy rice with both waxy and nonwaxy types. The protein content is higher in the waxy type and especially in upland rice. The content of oryzenin and albumin were likewise higher in the waxy and upland types. The results were discussed in the view point of nutrition.