• 한국작물학회:학술대회논문집
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• 한국작물학회 1988년도 춘계 학술대회지
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• pp.115-115
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• 1988

• Journal of Microbiology and Biotechnology
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• 제22권8호
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• pp.1054-1058
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• 2012

In order to predict biologically significant attributes such as function from protein sequences, searching against large databases for homologous proteins is a common practice. In particular, BLAST and HMMER are widely used in a variety of biological fields. However, sequence-homologous proteins determined by BLAST and proteins having the same domains predicted by HMMER are not always functionally equivalent, even though their sequences are aligning with high similarity. Thus, accurate assignment of functionally equivalent proteins from aligned sequences remains a challenge in bioinformatics. We have developed the FEP-BH algorithm to predict functionally equivalent proteins from protein-protein pairs identified by BLAST and from protein-domain pairs predicted by HMMER. When examined against domain classes of the Pfam-A seed database, FEP-BH showed 71.53% accuracy, whereas BLAST and HMMER were 57.72% and 36.62%, respectively. We expect that the FEP-BH algorithm will be effective in predicting functionally equivalent proteins from BLAST and HMMER outputs and will also suit biologists who want to search out functionally equivalent proteins from among sequence-homologous proteins.

• 아시안잔디학회지
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• 제5권1호
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• pp.11-22
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• 1991

This experiment was executed to investigate the possibility of the application of taxonomic method through the isoelectric focusing with polyacrylamide gel and sodium dodecyl sulfate-polyacrylamide gel electrophoresis with seeds in the identification of turfgrasses. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis was used to investigate the pattern of seed proteins which were extracted from 18 cultivars of cool season turfgrass and 4 cultivars of warm season turfgrass. The isoelectric focusing with polyacrylarnide gel was used to investigate the activity of the three isozymes of esterase, peroxidase and phosphoglucose isomerase which were extracted from 18 cultivars of cool season turfgrass and 4 cultivars of warm season turfgrass. The results were summarized as follows. 1. The difference of the patterns of seed proteins was observed with sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The identification of intra-genus was easily detected. 2. The three isozymes of esterase, peroxidase and phosphoglucose isomerase were investigated through isoelectric focusing with polyacrylamide gel. As a result, esterase was most effective among three isozymes in the identification of turfgrass cultivars 3. In the past cultivar identification was primarily based on visual morphological characters, but there was a lot of difficulty. If we should use electrophoresis, we will be able to identifvturfgrass cultivars more effectively.

• Journal of Ginseng Research
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• 제19권3호
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• pp.267-274
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• 1995

Vicilin and legumin, the storage Proteins of seed, were Purified from ginseng (Panax ginseng C.A. Meyer) endosperm cells. They were immunized in rabbits, and antibodies were raised respectively. Using these two antibodies, double immunogold labeling of vicilin and legumin was carried out to determine the gap of synthetic time and the transport pattern of vicilin and legumin in the ginseng endosperm cells. Vicilin and legumin were synthesized at the same time at early embryo developmental stage. They were secreted from the Golgi bodies and accumulated into the small vacuoles. As the endosperm cells developed, vicilin and legumin localized in the small vacuoles were gradually transported toward the large central vacuole where they were stored. Protein bodies were derived from the vacuoles filled with proteins and distributed in the endosperm cells of mature red seed. Protein bodies were various in size from 1 to 8 ${\mu}{\textrm}{m}$ in which vicilin and legumin were mixed each other. The number of small particles labeled on the vicilin was greater than that of large particles labeled on the legumin in the protein bodies indicating that the amount of vicilin is higher than that of legumin in the protein bodies.

• 한국작물학회지
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• 제10권
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• pp.91-97
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• 1971

춘파2조, 춘파6조 급 춘파6조대맥의 각:5품종 계 15품종의 종자단백질을 disc electrophoresis에 의하여 분리하고, 그 결과를 사진, densitometric tracing 급 모식도로 제시했다. 품종에 따라 18∼21 bands를 식별할 수 있었다. 품종은 각각 고유의 pattern을 보이고 있어, electrophoretic patter이 각품종의 유전적 차이를 반영하는 것이라고 생각된다. 추파대맥은 전부 희박한 B2 band를 갖이고 있고 춘파대맥은 농후한 B2 band를 갖이고 있었으며, 또 B2 band는 대파대맥에서, B3 band는 춘파대맥에서만 볼 수 있어, 춘파대맥과 추파대맥을 electrophoretic pattern에 의하여 구별할 수 있었다.

• 한국작물학회지
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• 제60권1호
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• pp.41-46
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• 2015

본 연구는 국내 육성 품종인 태광콩의 등숙기에 따른 단백질 발현 양상을 비교함으로써 등숙기 단백질 발현의 차이에 대한 기초자료를 얻고자 수행하였다. 동한 개화 후 종실의 등숙이 진행됨에 따라서 단백질 발현 양상이 세가지 경향으로 나뉘어 지는 것을 확인하였다. 첫 번째는 등숙이 진행됨에 따라서 단백질 발현 정도가 증가하다가 감소되며, 두 번째는 증가와 감소의 시기가 성숙기에 이루어지며, 세번째는 등숙기부터 성숙기까지 점진적으로 증가하는 것이다. 이러한 현상은 단백질의 기능에 따라 달라지는 것으로 사료된다. 등숙 초기에는 등숙에 필요한 단백질의 발현이 증가할 것이며 등숙 후기에는 저장단백질의 발현이 증가할 것으로 사료된다. 따라서 향후 좀 더 많은 수의 단백질 spot 들을 동정하여 어떤 기능을 가진 단백질이 등숙기에 따라 단백질의 발현 양상이 달라지는지는 좀 더 면밀히 관찰할 필요성이 있다고 사료된다.

• 한국작물학회:학술대회논문집
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• 한국작물학회 2004년도 춘계 학술대회지
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• pp.12-27
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• 2004

Thanks to spectacular advances in the techniques for identifying proteins separated by two-dimensional electrophoresis and in methods for large-scale analysis of proteome variations, proteomics is becoming an essential methodology in various fields of plant sciences. Plant proteomics would be most useful when combined with other functional genomics tools and approaches. A combination of microarray and proteomics analysis will indicate whether gene regulation is controlled at the level of transcription or translation and protein accumulation. In this review, we described the catalogues of the rice proteome which were constructed in our program, and functional characterization of some of these proteins was discussed. Mass-spectrometry is a most prevalent technique to identify rapidly a large of proteins in proteome analysis. However, the conventional Western blotting/sequencing technique us still used in many laboratories. As a first step to efficiently construct protein data-file in proteome analysis of major cereals, we have analyzed the N-terminal sequences of 100 rice embryo proteins and 70 wheat spike proteins separated by two-dimensional electrophoresis. Edman degradation revealed the N-terminal peptide sequences of only 31 rice proteins and 47 wheat proteins, suggesting that the rest of separated protein spots are N-terminally blocked. To efficiently determine the internal sequence of blocked proteins, we have developed a modified Cleveland peptide mapping method. Using this above method, the internal sequences of all blocked rice proteins (i. e., 69 proteins) were determined. Among these 100 rice proteins, thirty were proteins for which homologous sequence in the rice genome database could be identified. However, the rest of the proteins lacked homologous proteins. This appears to be consistent with the fact that about 30% of total rice cDNA have been deposited in the database. Also, the major proteins involved in the growth and development of rice can be identified using the proteome approach. Some of these proteins, including a calcium-binding protein that fumed out to be calreticulin, gibberellin-binding protein, which is ribulose-1,5-bisphosphate carboxylase/oxygenase activate in rice, and leginsulin-binding protein in soybean have functions in the signal transduction pathway. Proteomics is well suited not only to determine interaction between pairs of proteins, but also to identify multisubunit complexes. Currently, a protein-protein interaction database for plant proteins (http://genome .c .kanazawa-u.ac.jp/Y2H)could be a very useful tool for the plant research community. Recently, we are separated proteins from grain filling and seed maturation in rice to perform ESI-Q-TOF/MS and MALDI-TOF/MS. This experiment shows a possibility to easily and rapidly identify a number of 2-DE separated proteins of rice by ESI-Q-TOF/MS and MALDI-TOF/MS. Therefore, the Information thus obtained from the plant proteome would be helpful in predicting the function of the unknown proteins and would be useful in the plant molecular breeding. Also, information from our study could provide a venue to plant breeder and molecular biologist to design their research strategies precisely.

• 한국작물학회:학술대회논문집
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• 한국작물학회 2017년도 9th Asian Crop Science Association conference
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• pp.90-90
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• 2017

Regulation of seed dormancy is important in many grains to prevent pre-harvest sprouting. To identify and understand the gene related to seed dormancy regulation, we have screened for viviparous phenotypes of rice mutant lines generated by insertion of Ds transposon in a Korean Japonica cultivar (Dongjin) background. One of the mutants, which represented viviparous phenotype, was selected for further seed dormancy regulation studies and designated dor1. The dor1 mutant has single Ds insertion in the second exon of OsDor1 gene encoding glycine-rich protein. The seeds of dor1 mutant showed a higher germination potential and reduced abscisic acid (ABA) sensitivity compared to wild type Dongjin. Over-expression of Dor1 complements the viviparous phenotype of dor1 mutant, indicating that Dor1 function in seed dormancy regulation. Subcellular localization assay of Dor1-GFP fusion protein revealed that the OsDor1 protein mainly localized to membrane and the localization of OsDOR1 was influenced by presence of a giberelin (GA) receptor OsGID1. Further bimolecular fluorescence complementation (BiFC) analysis indicated that OsDOR1 interact with OsGID1. The combined results suggested that OsDOR1 regulates seed dormancy by interacting with OsGID1 in GA response. Additionally, expression of OsDOR1 partially complemented the cold sensitivity of Escherichia coli BX04 mutant lacking four cold shock proteins, indicating that OsDOR1 possessed RNA chaperone activity.

• 한국환경농학회지
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• 제32권1호
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• pp.48-54
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• 2013

수수 종자의 품종 간 특이적으로 발현하는 단백질을 동정하여 기능성 유전자를 확보하고 이들 유전자를 이용하여 수수의 기능성 강화 및 품종 판별 기술 개발을 위한 유용 유전자를 확보하고자 프로테오믹스 기법을 이용하여 수수 종자로부터 단백질을 추출하였다. 추출한 단백질을 이차원전기영동후, colloidal CBB 염색을 통해 품종 별로 발현에 차이를 보이는 단백질을 분석하였다. 총 652 개의 spot들 중에 8개의 단백질 spot들이 발현 정도에 변화를 보였으며, 이들 단백질을 MALDI-TOF/TOF MS와 MASCOT database를 통해 동정한 결과, RNA metabolism (spot 1, spot 4) HSP (spot 2), 저장 단백질 (spot 3, spot 5, spot 6), 산화-환원 (spot 8) 관련 단백질 등이 동정되었다. 특히 동정된 단백질은 주로 흰찰수수 (WCS)에서 발현 정도가 높게 나오는 경향을 보였으며, 흰찰수수 (WCS)에서 유일하게 발현 되는 단백질로 Cupin family protein, Gloubulin 등이 동정되었다. DEAD-box helicase는 흰찰수수 (WCS)를 제외한 나머지 세 품종에서 발현되었다. Ribonuclease T2와 Aldo-Keto reductase는 대풍수수 (DPS)를 제외한 나머지 세 품종에서 발현되었다. HSPs는 토종수수 (TJS)에서만 발현 되는 것을 확인하였다. 이들 동정된 단백질들은 수수의 품종 별 특성을 이해하는데 중요한 단서를 제공할 것으로 예측된다.

• 한국식품위생안전성학회지
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• 제6권1호
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• pp.67-72
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• 1991

어묵에 grapefruit 종자 추출물의 농도별로, 침지 처리한 후 저장기간에 따른 물리, 화학적 변화를 검토하여 다음과 같은 결과를 얻었다. 1. 저장 기간 중 어묵의 조단백함량 변화는 대조구에 비하여 GFSE 의 처리 농도가 높을수록 더 작았다. 2. Texture 는 저장기간이 경과함에 따라 감소하는 경향을 나타내었으나 GFSE 용액 처리구에서는 감소율이 낮았다. 3 어묵 단백질의 SDS-PAGE pattern 변화는 저장기간이 경과함에 따라 분자량, 30,000-32,000의 protein은 점차 가수분해되어 소멸되는 현상을 보였으며 특히 대조군의 경우 2일 경과 후부터 급격한 분해라 이루어져 단백질 major band의 손실율이 크게 증가한 것으로 나타난 반면, GFSE처리 시험구의 경우 4일 경과시에야 비로소 뚜렷한 손실반응을 보여 GFSE처리에 의하여 어묵단백질의 변패 발생 시기를 상당 기간 연장함을 확인할 수 있다.