• Reproductive and Developmental Biology
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• v.37 no.4
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• pp.247-253
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• 2013

Here, we present an approach of blood plasma proteome profiling and their comparisons between the young and the adult pigs as prerequisite for the identification of bio-markers related to the health conditions, growth performance and meat quality. To profile the proteome in porcine plasma, blood samples were collected from 19 young piglets and 20 adult male barrows and the plasma was retrieved. Then, protein profiling was initiated using one and two-dimensional electrophoresis. Proteins were spotted and then identified by MALDI-TOF-TOF and LC-MS-MS. In the results, more than thirty-six and twenty eight protein spots were selected in young piglets and adult pigs, respectively and twenty three proteins were identified. The proteome profile images were compared between those ones using Image Master Version 7.0. The image of expressed proteome showed that most of proteins from plasma of young piglet separated clearly and concentrated in 2DE display compared to ones from adult. Image analysis in detail was carried out to look for the specific proteins related to age progression. It demonstrated that the characteristics of proteome expression could be distinct to their age stages. Further investigations needed to proceed to understand the age dependent change of protein conformation and biological meaning of those differences in proteome expression between young and mature adult pigs.

• Proceedings of the Korean Magnetic Resonance Society Conference
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• 2002.08a
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• pp.87-87
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• 2002

• Proceedings of the Korean Magnetic Resonance Society Conference
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• 2002.08a
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• pp.86-86
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• 2002

• Bulletin of the Korean Chemical Society
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• v.27 no.9
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• pp.1456-1458
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• 2006

• BMB Reports
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• v.37 no.1
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• pp.45-52
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• 2004

The goal of interaction proteomics that studies the protein-protein interactions of all expressed proteins is to understand biological processes that are strictly regulated by these interactions. The availability of entire genome sequences of many organisms and high-throughput analysis tools has led scientists to study the entire proteome (Pandey and Mann, 2000). There are various high-throughput methods for detecting protein interactions such as yeast two-hybrid approach and mass spectrometry to produce vast amounts of data that can be utilized to decipher protein functions in complicated biological networks. In this review, we discuss recent developments in analytical methods for large-scale protein interactions and the future direction of interaction proteomics.

• Journal of Microbiology and Biotechnology
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• v.11 no.6
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• pp.1111-1114
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• 2001

An extracellular fibrinolytic-enzyme-producing bacterium was isolated from Doen-Jang, a Korean traditional fermented flood, and identified as Bacillus sp. DJ based on its morphology and cellular fatty acid composition. The total extracellular fibrinase (EF) from Bacillus sp. DJ was analyzed using three fibrin zymographic techniques, SDS-fibrin zymography (SDS-FZ), isoelectrofocucing-fibrin zymographs(IEF-FZ), and a two-dimensional SDS-fibrin zymographic analysis (2D SDS-FZ). As a result, the EP map of Bacillus sp. DJ was established. The results suggest that the 2D SDS-FZ method will be a useful tool for the proteomic approach for many other bacterial pretenses.

• Proceedings of the Korean Society for Bioinformatics Conference
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• 2005.09a
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• pp.91-95
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• 2005

In the multidimensional protein identification technology of high-throughput proteomics, we use one-dimensional gel electrophoresis and after the separation by two-dimensional liquid chromatography, the sample is analyzed by tandem mass spectrometry. In this study, we have analyzed the Pseudomonas Putida KT2440 protein. From the protein identification, the protein database was combined with its reversed sequence database. From the peptide selection whose error rate is less than 1%, the SEQUEST database search for the tandem mass spectral data identified 2,045 proteins. For each protein, we compared the molecular weight calibrated from 1D-gel band position with the theoretical molecular weight computed from the amino acid sequence, by defining a variable MW$_{corr}$ Since the bacterial proteome is simpler than human proteome considering the complexity and modifications, the proteome analysis result for the Pseudomonas Putida KT2440 could suggest a guideline to build the protocol to analyze human proteome data.

• BMB Reports
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• v.35 no.2
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• pp.236-238
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• 2002

Based on the zymography analysis, Bacillus sp. DJ-4 (screened from Doen-Jang, a Korean traditional fermented food) secretes seven extracellular fibrinolytic enzymes (EFEs; 68, 64, 55, 45, 33, 27, and 13 kDa) in culture broth. These seven EFEs were analyzed by newly applied SDS-fibrin zymography combined with gradient polyacrylamide (SDS-FZGP). This improved gel system was used with a 5-20% acrylamide gradient in a fibrin zymogram gel for the separation of proteins with molecular masses from below 10kDa to over 100kDa on one gel plate. Using this system, high molecular weight bands (HMWBs) were clearly and sharply resolved. We also examined the relationship between an acrylamide concentration and the enzymatic activity of EFE using densitometric analysis.

• Journal of Microbiology and Biotechnology
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• v.17 no.12
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• pp.2005-2017
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• 2007

Diabetic nephropathy remains a major cause of morbidity and mortality in the diabetic population and is the leading cause of end-stage renal failure. Despite current therapeutics including intensified glycemic control and blood pressure lowering agents, renal disease continues to progress relentlessly in diabetic patients, albeit at a lower rate. Since synthetic drugs for diabetes are known to have side effects, fungal mushrooms as a natural product come into preventing the development of diabetes. Our previous report showed the hypoglycemic effect of extracellular fungal polysaccharides (EPS) in streptozotocin (STZ)-induced diabetic rats. In this study, we analyzed the differential expression patterns of rat kidney proteins from normal, STZ-induced diabetic, and EPS-treated diabetic rats, to discover diabetes-associated proteins in rat kidney. The results of proteomic analysis revealed that up to 500 protein spots were visualized, of which 291 spots were differentially expressed in the three experimental groups. Eventually, 51 spots were statistically significant and were identified by peptide mass fingerprinting. Among the differentially expressed renal proteins, 10 were increased and 16 were decreased significantly in diabetic rat kidney. The levels of different proteins, altered after diabetes induction, were returned to approximately those of the healthy rats by EPS treatment. A histopathological examination showed that EPS administration restored the impaired kidney to almost normal architecture. The study of protein expression in the normal and diabetic kidney tissues enabled us to find several diabetic nephropathy-specific proteins, such as phospholipids scramblase 3 and tropomyosin 3, which have not been mentioned yet in connection with diabetes.

• BMB Reports
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• v.34 no.6
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• pp.531-536
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• 2001

Three zymographic techniques using casein, fibrin, and gelatin as substrates in SDS-PAGE were compared based on three aspects: (1) The proteolytic pattern of extracellular enzymes from the three bacterial strains, Bacillus sp. DJ-1, DJ-2, and DJ-3. (2) The enzymatic sensitivity of their activity on zymogram gels. (3) The stability of stained zymogram gels with Coomassie brilliant blue in the destaining solution. There was no significant difference on the pattern of extracellular enzymes from the three strains. The bands in the fibrin gel were clearer and more distinct from the extensive destaining process. It was also shown that the gelatin gel revealed the highest enzymatic sensitivity among the three gels, based on the densitometric analysis. In the casein gel, a trace that could be mistaken as a proteolytic band appeared around 40-50 kDa.