• Biotechnology and Bioprocess Engineering:BBE
• /
• v.8 no.2
• /
• pp.89-93
• /
• 2003

human renin binding protein (hRnBp), showing N-acetylglucosamine-2-epimerase activity, was over-expressed in E. coli, but was mainly present as an inclusion body. To improve its solubility and activity, ubiquitin (Ub), thioredoxin (Trx), maltose binding protein (MBP) and NusA, were used as fusion partners. The comparative solubilities of the fusion proteins were, from most to least soluble: NusA, MBP, Trx, Ub. Only the MBP fusion did not significantly reduce the activity of hRnBp, but enhanced the stability. The Origami (DE3), permitting a more oxidative environment for the cytoplasm in E. coli; helped to increase its functional activity.

• 한국생물공학회:학술대회논문집
• /
• 2003.04a
• /
• pp.539-542
• /
• 2003

Fusion gene of GFPuv and Cytochrome c-552 was inserted into the pTrcHis B vector and transferred to E. coli. A fusion protein of GFPuv and Cytochrome c-552 was expressed in BL21. This fusion protein was composed of a His-tag for purification using an immobilized metal affinity chromatography(IMAC). IMAC constitutes a rather facile means of unravelling the principles of recognition and, in particular, of identifying the counterligands on the protein surface, which interact with the ligated and immobilized metal ions. Histidine when present on the surface of a protein molecule under a favorable solvent condition, may serve as electron donors in coordination with the immobilized chelates of some transition metal ions$(Ni^{2+})$.

• BMB Reports
• /
• v.37 no.1
• /
• pp.133-138
• /
• 2004

Proteomics is a leading technology for the high-throughput analysis of proteins on a genome-wide scale. With the completion of genome sequencing projects and the development of analytical methods for protein characterization, proteomics has become a major field of functional genomics. The initial objective of proteomics was the large-scale identification of all protein species in a cell or tissue. The applications are currently being extended to analyze various functional aspects of proteins such as post-translational modifications, protein-protein interactions, activities and structures. Whereas the proteomics research is quite advanced in animals and yeast as well as Escherichia coli, plant proteomics is only at the initial phase. Major studies of plant proteomics have been reported on subcellular proteomes and protein complexes (e.g. proteins in the plasma membranes, chloroplasts, mitochondria and nuclei). Here several plant proteomics studies will be presented, followed by a recent work using multidimensional protein identification technology (MudPIT).

• Journal of Microbiology and Biotechnology
• /
• v.3 no.4
• /
• pp.261-265
• /
• 1993

A sopA protein (41K) encoded by plasmid pXX288 was observed in the cytoplasm, whereas a sopB protein (37K) encoded by plasmid pXX157 was observed in the membrane fraction. Most of the sopB protein was solubilized from the crude membrane by treatment with Sarkosyl, which suggested that the protein may be located in the inner membrane. The sopA protein was precipitated at the concentration of 30 to 60% ammonium sulfate. The sedimentation profile of the crude membrane fraction showed a little difference according to culture media used, and the sopB protein existed in all fractions of inner membrane. The DNA of plasmids, pXX157, pXX300, and pXX167 co-sedimented with inner membrane fraction.

• Journal of Plant Biology
• /
• v.37 no.3
• /
• pp.357-363
• /
• 1994

An expreiment with non-nodulating alfalfa (Medicago sativa L.) plants was designed to investigate the changes in protein contents and the activities of proteolytic enzymes during a regrowth period of 24 d. Shoot removal caused a depression of root growth and significantly reduced protein contents in roots. An initial decline of root proteins for the first 10 d was followed by a rapid recovery from d 11 to 24. The major increase of regrowing shoot weight occurred also from d 11. The activities of aminopeptidase and endoprotease slightly decreased in regrowing leaves, while protein contents remains stable after shoot removal. Roots exhibited source behaviour with a rapid increase of endoprotease activities for the first 10 d of regrowth; about a 370% increase over the initial level was observed. Increase in endoprotease activity in roots coincided with the time of protein remobilization after shoot removal, indicating the important role of endoproteases in protein degradation.

• Journal of the Korean Society of Clothing and Textiles
• /
• v.21 no.6
• /
• pp.970-976
• /
• 1997

Synthetic leather added collagen protein was coagulated in DMF solution. With increasing collagen concentration, thickness of synthetic leather increased. In addition, water vapor permeability and water vapor absoption increased with increasing collagen protein concentration. But MIU and SMD value of surface properties decreased with increasing collagen protein concentration. As a result, synthetic leather added collagen protein showed comfort and dry touch.

• Journal of the Korean Data and Information Science Society
• /
• v.15 no.4
• /
• pp.1019-1031
• /
• 2004

This paper describes a new modeling method for the prediction of transmembrane protein topology. The structural regions of the transmembrane protein have been modeled by means of a multiple state hidden Markov model that has provided for the detailed modeling of the heterogeneous amino acid distributions of each structural region. Grammatical constraints have been incorporated to the prediction method in order to capture the biological order of membrane protein topology. The proposed method correctly predicted 76% of all membrane spanning regions and 92% sidedness of the integration when all membrane spanning regions were found correctly.

• Korean Journal of Poultry Science
• /
• v.30 no.2
• /
• pp.113-118
• /
• 2003

In this study, broilers were raised up to 6 weeks of age in a single room to determine if different levels of dietary protein or addition of aluminum sulfate[alum, $Al_2$(SO$_4$)$_3$ㆍ14$H_2O$] to the litter affected growth performance, production of ammonia(NH$_3$) and soluble phosphorus(SP) content of the litter.The experimental treatments consisted of six treatments in a 2x3 factorial arrangements: T$_1$＝23% protein ＋ 0.2% alum to litter; T$_2$＝21% protein ＋ 0.2% alum to litter; T$_3$＝19% protein ＋ 0.2% alum to litter; T$_4$＝23% protein ＋ no alum; T$_{5}$＝21% protein ＋ no alum; T$_{6}$＝19% protein ＋ no alum. For broiler performance, there was no effect of alum addition to the litter, but the dietary protein levels significantly affected feed intake from days 22 to 42(P<0.05) and day 0 to 42(P< 0.05), weight gain during all periods(P<0.05 or 0.01), and feed:gain from day 0 to 21(P<0.05) and day 0 to 42(P<0.05). Alum addition to the litter did not affect body weight at 21 and 42 days, but dietary protein levels has a significant effect on it at both 21(P<0.0l) and 42 days(P<0.05). Alum addition only affected ammonia production at weeks 3(P

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.22 no.2
• /
• pp.127-131
• /
• 1993

To evaluate an effect of dietary protein on lipoprotein profile serum of carbon tetrachloride-treated rats, carbon tetrachloride (50% in olive oil) was twice given at 0.1ml/100g body weight at intervals of 24hours to the male rats and then the degree of liver damage in carbon tetrachloride-treated animals fed a low protein diet was compared with that fed a high protein diet. The increasing rate of liver weight/body weight and the serum levels of alanine aminotransferase in carbon tetrachloride-treated rats to the control group were higher in rats fed high protein diet than those fed low protein diet. In the serum levels of lipid (total lipid, total cholesterol and triglyceride) remarkable differences were not found between low protein diet group and high protein diet group. But these serum lipids in carbon tetrachloride-treated rats were decreased and the decreasing rate of serum lipids to control group were higher in carbon tetrachloride-treated rats fed high protein diet than those fed low protein diet. Under the animal model as identified by the present data herein, serum pre $\beta$-lipoprotein and $\alpha$-lipoprotein fractions were decreased in carbon tetrachloride-treated rats, but the serum levels of $\beta$-lipoprotein were rather increased in the both group by the injection of carbon tetrachloride. Especially, the decreasing rate of $\alpha$-lipoprotein fraction was higher in $CCl_4$-treated rats fed a high protein diet than those fed a low protein diet to its control group and the increasing rate of serum $\beta$-lipoprotein fraction was also higher in $CCl_4$-treated rats fed high protein diet than those fed low protein diet.

• KOREAN JOURNAL OF CROP SCIENCE
• /
• v.53 no.spc
• /
• pp.78-83
• /
• 2008

Soybean [Glycine max (L.)] is a major source of protein for human and animal feed. Inter- and intra-genotype variation of soybean protein has been investigated by soybean researchers. However, limited sample amount of soybean single seed there is no report that investigated intra-plant variation of soybean protein within soybean plant. Recently a non-destructive NIR (near-infrared reflectance) spectroscopy using single seed grain to analyze seed protein was developed. The objectives of this study were to understand variation of seed protein content within plant and to determine the amount of minimum sample size which can represent protein content for a soybean plant. Frequency distribution of protein content within plant showed normal distribution. There was an intra-cultivar variation for protein content in soybean cultivar Seonnogkong. Difference of protein content among single plants of Seonnokong was recognized at 5% level. Seeds in lower position on plant stem tended to accumulate more protein than in higher position. There was significant difference for protein content between sample size 5 seeds and sample size of more than 5 seeds (10, 20, 30, 40, and 50 seeds) at a soybean plant with 57 seeds however no difference was recognized among sample size (5, 10, 20, and 30 seeds) at a soybean plant with 33 seeds. Around 20% seeds of soybean from single plant needed to determine the protein content to represent protein content of single soybean plant. This study is the first one to report evidence of intra-plant variation for proteincontent which detected by non-destructive NIR spectroscopy using single seed grain in soybean.