• KOREAN JOURNAL OF CROP SCIENCE
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• v.49 no.2
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• pp.141-147
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• 2004

This study was carried out to know the variation of soybean seed proteins, 11S and 7S globulins, and their amino acid compositions among different colored soybean varieties, 'Danbaegkong' (yellow), 'Pureunkong' (green) 'Jinyulkong' (brown), and 'Geoumjeongkong l' (black). Soybean seed proteins showed a wide range in molecular size, but the electrophoresis patterns of total seed protein subunits showed a similarity among different colored soybean varieties. Amino acid compositions of total seed proteins were similar for all soybean varieties tested. However, soybean varieties showed low composition rates in sulfur containing amino acids. The composition rates of cysteine and methionine in the 11S globulins were higher than those of total seed proteins and 7S globulins. Glutamic acid and glycine were higher in the 11S and 7S globulins than those of total seed proteins. However, the levels of methionine and phenylalanine are high in the 11S globulins, but those of valine and lysin are slightly lower than the 7S globulins. By using HPLC, we tried to analyse the soybean seed proteins. The 11S globulin was composed of 10 major peaks whereas the 7S globulin was composed of 4 major peaks. The composition rates of 11S related proteins have a tendency to increasing during the maturing whereas those of 7S related proteins have a tendency to decreasing. Composition rates of each peaks among different colored soybean varieties suggested that soybean seed proteins are varied, although they showed similarity in the electrophoresis patterns, and understanding of this characteristics is important for the utilization of soybeans.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.60 no.1
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• pp.29-32
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• 2015

Two-dimensional electrophoresis (2-DE) was executed to separate the seed storage proteins from the buckwheat. The proteins extracted from the whole seed proteins were better separated and observed in the use of lysis buffer. Using this method, the highly reproducible isoelectric focusing (IEF) can be obtained from polyacrylamide gels, and IEF from the polyacrylamide gel at all the possible pH range (5.0-8.0) was more easily separated than IPG (immobilized pH gradient) gels. The polyacrylamide gels in the first dimension in 2-DE was used to separate and identify a number of whole seed proteins in the proteome analysis. In this new apparatus using 2-DE, 27cm in length of plate coated with polyacrylamide gel was used and the experiment was further investigated under the various conditions.

• Journal of the Korean Society of Food Science and Nutrition
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• v.17 no.1
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• pp.43-49
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• 1988

The proteins of peach seed four was examined to utilize protein source. The peach seed flour contained 20.38% of crude proteins. The extractability of salt souble proteins of seed were 70% and recovery rate of main protein fractions separated by sephadex G-200 were about 51%. The electrophoretic analysis showed 11 bands and molecular weight showed 14,000-110,000 in seed proteins. The Amino acid of peach seed flour and isolated were mainly composed of arginine, asparic acid. glutamic acid, glycine and leucine. The solubility of isolated peach seed protein was lowest at pH 5.5.

• Journal of Plant Biotechnology
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• v.47 no.2
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• pp.118-123
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• 2020

The black seed coat of soybeans contain anthocyanins which promote health. However, mature soybean seeds contain anti-nutritional factors like lipoxygenase, lectin and Kunitz Trypsin Inhibitor (KTI) proteins. Furthermore, these seeds can be used only after the genetic elimination of these proteins. Therefore, the objective of this study was to develop novel soybean genotypes with black seed coat and triple recessive alleles (lx1lx1lx2lx2lx3lx3, titilele) for lipoxygenase, lectin, and KTI proteins. From a cross of parent1 (lx1lx2lx3/lx1lx2lx3, ti/ti, Le/Le) and parent2 (lx1lx2lx3/lx1lx2lx3, Ti/Ti, le/le), 132 F₂ seeds were obtained. A 3:1 segregation ratio was observed during F₂ seed generation for the inheritance of lectin and KTI proteins. Between a cross of the Le and Ti genes, the observed independent inheritance ratio in the F₂ seed generation was 9: 3 : 3 : 1 (69 Le_Ti_: 32 leleTi_: 22 Le_titi: 9 leletiti) (χ²=2.87, P=0.5 - 0.1). From nine F₂ seeds with triple recessive alleles (lx1lx1lx2lx2lx3lx3, titilele genotype), one novel strain posessing black seed coat, and free of lipoxygenase, lectin and KTI proteins, was selected. The seed coat color of the new strain was black and the cotyledon color of the mature seed was green. The weight of 100 seeds belonging to the new strain was 35.4 g. This black soybean strain with lx1lx1lx2lx2lx3lx3, titilele genotype is a novel strain free of lipoxygenase, lectin, and KTI proteins.

• Korean Journal of Plant Resources
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• v.22 no.3
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• pp.227-235
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• 2009

Single seeds of common buckwheat cultivar Suwon No. 1 when subjected to SDS-PAGE revealed very high polymorphism. High variation existed for protein or protein subunits with molecular weight 54-47kDa, 45-25kDa and 16-11kDa. The electrophoregram showed variation for globulin as well as other protein fractions. About 300 proteins were separated by two-dimensional electrophoresis in common buckwheat (Fagopyrum esculentum Moench.) seed. Seed maturation is a dynamic and temporally regulated phase of seed development that determines the composition of storage proteins reserves in mature seeds. Buckwheat seeds from 5, 10, 15, 20, and 25 days after pollination and matured stage were used for the analysis. This led to the establishment of high-resolution proteome reference maps, expression profiles of 48 spots. It was identified 48 proteins from MALDI-TOF/MS analysis of wild buckwheat seed storage proteins. The 48 proteins were found identical or similar to those of proteins reported in buckwheat and other plants; it is belonging to 9 major functional categories including seed storage proteins, stress/defense response, protein synthesis, photosynthesis, allergy proteins, amino acid, enzyme, metabolism, and miscellaneous. It appears that the major allergenic storage protein separated played the important role in buckwheat breeding and biochemical characterization.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.59 no.3
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• pp.359-363
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• 2014

Soybean seed is a good source of plant protein in human consumables such as baby formula and protein concentrate. The seeds contain an abundance of storage proteins, namely ${\beta}$-conglycin and glycinin that account for ~ 70-80% of the total seed protein content. Proteome profiling has been proved to be an efficient way that can help us to investigate the seed storage proteins. In the present study, the seeds were removed from the pods and the cotylendonary tissues were separated from the testa for proteome analysis in order to investigate the seed storage proteins. A systematic proteome profiling was conducted through one-dimensional gel electrophoresis followed by MALDI-TOF-TOF mass spectrometry in the seeds (cotyledonary tissue) of soybean genotypes. Two dimensional gels stained with CBB, a total of 10 proteins were identified and analyzed using MASCOT search engine according to the similarity of sequences with previously characterized proteins along with the UniProt database. A total of ten proteins such as glycinin Gy4 precursor, glycinin G3 precursor, glycinin G1 precursor, glycinin chain A2B1a precursor, glycinin chain A2B1a precursor were identified in our investigation. However, the glycinin subunit may be considered to play important roles in soybean breeding and biochemical characterization. In addition, the improved technique will be useful to dissect the genetic control of glycinin expression in soybean.

• Asian Pacific Journal of Cancer Prevention
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• v.14 no.8
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• pp.4621-4625
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• 2013

The purpose of this study was to construct a protein-protein interaction (PPI) network related to oral squamous cell carcinoma (OSCC). Each protein was ranked and those most associated with OSCC were mined within the network. First, OSCC-related genes were retrieved from the Online Mendelian Inheritance in Man (OMIM) database. Then they were mapped to their protein identifiers and a seed set of proteins was built. The seed proteins were expanded using the nearest neighbor expansion method to construct a PPI network through the Online Predicated Human Interaction Database (OPHID). The network was verified to be statistically significant, the score of each protein was evaluated by algorithm, then the OSCC-related proteins were ranked. 38 OSCC related seed proteins were expanded to 750 protein pairs. A protein-protein interaction nerwork was then constructed and the 30 top-ranked proteins listed. The four highest-scoring seed proteins were SMAD4, CTNNB1, HRAS, NOTCH1, and four non-seed proteins P53, EP300, SMAD3, SRC were mined using the nearest neighbor expansion method. The methods shown here may facilitate the discovery of important OSCC proteins and guide medical researchers in further pertinent studies.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.40 no.4
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• pp.407-412
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• 1995

Experiments were conducted to obtain information on separation of nonviable seeds from seed lots by the nondestructive ways. Seeds of sesame, welsh onion and lettuce were artificially aged at 90% relative humidity and 45$^{\circ}C$ to get different seed qualities. The relationships between seed quality and leakage of total sugars, amino acids, and proteins into soaking water were determined to know a possibility of grading seeds. Dead seeds of lettuce leaked significant amounts of total sugars, amino acids, and proteins, while high quality seeds leaked negligeable amounts of total sugars and some of amino acids and proteins. Dead seeds of welsh onion leaked significant amounts of amino acids and some total sugars and proteins, while high quality seeds leaked negligeable amounts of these compounds. Sesame seeds leaked little total sugars, amino acids, and proteins regardless of seed quality.

• Korean Journal of Plant Tissue Culture
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• v.27 no.4
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• pp.283-297
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• 2000

Seeds are an ideal repository for recombinant proteins in molecular farming applications. However, in order to use plant seeds efficiently for the production of such proteins, it is necessary to understand a number of fundamental biological properties of seeds. This includes a full understanding of promoters which function in a seed-specific manner, the subcellular targeting of the desired polypeptide and the final form in which a protein is stored. Once a biologically active protein has been deposited in a seed, it is also critical that the protein can be extracted and purified efficiently. In this review, these issues are examined critically to provide a number of approaches which may be adopted for production of recombinant proteins in plants. Particular attention is paid to the relationship between subcellular localization and protein extraction and purification. The robustness and flexibility of seed-based production is illustrated by examples close to or already in commercial production.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.62 no.1
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• pp.40-50
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• 2017

Seed storage proteins are used as carbon and nitrogen sources for the nutritional improvement of seeds. Since the composition of proteins from the Korean cultivars of proso millet is unknown, this study was conducted to obtain a reference map of millet seed proteins and identify the functional characteristics of the identified proteins. Proteins extracted from proso millet seeds of various cultivars were investigated using proteomic techniques such as 2-D electrophoresis coupled with mass fingerprinting; 1152 (differentially expressed) protein spots were detected on the 2-D gels. Among them, 26 reproducible protein spots were analyzed using matrix-assisted laser desorption/ionization time-of-flight/time-of-flight mass spectrometry. Out of the 26 proteins, 2 proteins were upregulated in all the millet cultivars, while 13 proteins were upregulated and 11 proteins were downregulated in 2 cultivars. Abundance of most of the identified protein species associated with polysaccharide and starch metabolism, transcription, and pathogenesis was significantly enhanced, while that of other protein species involved in glycolysis, stress response, and transduction was severely reduced. Taken together, the results suggest that the differential expression of the proteins from the four millet cultivars may be cultivar-specific. By conducting a proteomic investigation of millet seeds from different cultivars, we sought to better understand the functional categorization of individual proteins on the basis of their molecular functions. We believe that the identified proteins may help in investigating genetic variations in millet cultivars.