• Biomedical Science Letters
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• v.16 no.1
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• pp.19-24
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• 2010

We analyzed and compared the concentration of total cholesterol (CHOL), high density lipoprotein (HDL) cholesterol, low density lipoprotein (LDL) cholesterol and triglyceride (TG) in serum and the serum protein electrophoresis fractions of thyroid disease patients. In comparison with the average of reference, our data showed that the average concentration of CHOL, LDL cholesterol and TG in hyperthyroidism patients were decreased significantly, but HDL cholesterol was increased significantly. In hypothyroidism patients, CHOL, HDL cholesterol, LDL cholesterol and TG were all increased significantly. In comparison of the concentration of lipids in each patient to reference range, 28.3% of hyperthyroidism patients showed abnormally low level of total cholesterol. In the patients with hypothyroidism, the percentage of patients showed abnormally high level of CHOL, HDL cholesterol, LDL cholesterol and TG were 37.7%, 10%, 68.8% and 49.1%, respectively. In our studies of serum protein electrophoresis, the average of ${\alpha}_2$-globulin and $\gamma$-globulin in hyperthyroidism patients were increased and $\beta$-globulin was decreased significantly. In hypothyroidism patients, the average of $\gamma$-globulin was increased and $\beta$-globulin was decreased significantly. In comparison of protein fractions of each patient to reference range, 38.3% and 50.0% of hyperthyroidism patients showed abnormally high levels of ${\alpha}_2$-globulin and $\gamma$-globulin, but 73.3% of patients showed abnormally low level of $\beta$-globulin. In hypothyroidism patients, 70.4% of patients were abnormally decreased in $\beta$-globulin and 63.9% of patients were abnormally increased in $\gamma$-globulin. These data suggest that the concentrations of CHOL, HDL cholesterol, LDL cholesterol and TG are not critical data for clinical interpretation of hyperthyroidism, but the levels of them are useful for interpretation of hypothyroidism patients. Our results of serum protein electrophoresis suggest that the concentration of serum protein electrophoresis fractions can be useful to understand the thyroid disease.

• International Journal of Industrial Entomology and Biomaterials
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• v.14 no.1
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• pp.37-44
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• 2007

A study was made of the haemolymph protein spectrum of mulberry silkworm (Bomhyx mori L.) from the first larval instar to imago. Horizontal starch gel electrophoresis was used. Sixteen races and eight F1 interracial hybrids, raised in Bulgaria, were analyzed. During the ontogenesis, a total of 17 protein bands (15 cathodic and 2 anodic) were detected. Distinct dynamics in the haemolymph protein spectrum was observed, in result of different expression during the individual development associated with the processes of growth, histolysis and histogenesis. Based on the ontogenetic dynamics found, a correspondence was assumed between some proteins detected by us using the starch gel electrophoresis and major haemolymph proteins (SP1, SP2, MHPs and Vg) detected by other authors using the polyacrilamide gel electrophoresis. Intraracial and interracial polymorphism was observed in four protein zones. The effect of four polymorphic loci with codominant and null alleles was suggested.

• BMB Reports
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• v.31 no.6
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• pp.542-547
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• 1998

The main function of adipocytes in various species is to store nutrient energy in the form of triglycerides, and this function may he closely related with hormonal signaling through the plasma membrane of adipocytes. Using SDS-PAGE, two-dimensional gel electrophoresis, and a membrane biotinylation technique, we have identified a 55KDa protein (55K protein) from the plasma membrane fraction of adipocytes, with an isoelectric point (pI) of 8.1-8.3. However, this 55K protein was not observed with a two-dimensional gel electrophoresis carried out on plasma membrane fractions prepared from the liver, heart, and kidney tissues. An analysis of the 12 amino acids sequence at the N-terminal of the 55K protein showed that it has a similar sequence to that of bovine serum albumin.

• Journal of Life Science
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• v.9 no.1
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• pp.35-39
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• 1999

Elecrophoreticl analysis of a 36 kDa protein was runned by SDS-PAGE, isoelectric focusing (IEF) and two dimensional electrophoresis pattern. Major 36 kDa and 25, 46, 48, 66 kDa protein were detected by Coomassie blue stain on SDS-PAGE. Major 36kDa protein was eluted for production of antiserum for serological analysis, IEF and two dimensional electrophoresis. Isoelectric point of 36kDa was aout pH 8.5. Two dimensional electrophoresis of eluted 36kDa showed one point on the gel. Anti-36 kDa serum made by newzilland rabbit for serological test. In ELISA, final titer of antibody was 100×{TEX}$2^5}${/TEX} : 1. Neutralize ability of serum was examined by slide agglutination test and colonization test in rat. Anti-36 kDa serum agglutinated whole cell of V. vulnificus were inhibited colonization on intestine in rat. Accordingly In this paper contain some electrophoretical analysis and serological test of a 36 kDa OMP of V. vulnificus.

• Bulletin of the Korean Chemical Society
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• v.35 no.9
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• pp.2621-2624
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• 2014

The rapid and spontaneous adsorption of proteins on nanoparticle (NP) surfaces in biological fluids such as blood is an important phenomenon as it possibly determines "what the cells see" and, thus, the fates of NPs in living organisms. In order to quantitatively understand protein coronas at the molecular level, we investigated human serum albumin (HSA) coronas that were produced on silica NPs of 20 nm and 50 nm diameters using conventional gel electrophoresis. Analysis of the concentration dependence of protein adsorption showed that HSA coronas preferentially formed a monolayer on silica NPs and revealed the presence of hard protein coronas. HSA adsorption was clearly dependent on NP size, and this might be due to the different surface curvatures of NPs of different sizes.

• International Journal of Industrial Entomology and Biomaterials
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• v.17 no.2
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• pp.217-221
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• 2008

Dung beetle larvae at the $3^{rd}$ instar were injected with lipopolysaccaride and inducible proteins were examined within a pI level of 3-10 and a size level by proteomics, including 1-D SDS PAGE analysis and antibacterial assay. The immune infected larvae extracts provided seven protein bands in one-dimensional electrophoresis and its antibacterial activity also checked. Hemolymph protein from immune infected larvae of the dung beetle were separated by twodimensional gel electrophoresis and compared with those from native larvae. In 2-D gel electrophoresis, we detected 63 immune infected unique and 32 up-regulated proteins, and 36 proteins that were down-regulated or not present in treated gel. Ten protein spots from unique proteins and those presented as different level of abundance in infected and native larvae were specially expressed. These differentially expressed proteins were proposed to be involved in the defense mechanism against microorganism.

• Biomedical Science Letters
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• v.10 no.3
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• pp.253-257
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• 2004

The mechanisms by which leptospires caused disease are not well understood. A number of putative virulence factors have been suggested, but with few exceptions their role in pathogenesis remains unclear. In these days, many cases of leptospirosis are diagnosed by serological immunoassay. Leptospirosis is characterized by the histopathology of liver, kidney, heart, and lung, but the electrophoresis fractions of serum protein are not compared. We analyzed total protein, albumin, aspartic aminotranferase (AST), alanine aminotransferase (ALT), alkaline phosphatase (ALP), creatinine and urea nitrogen (UN) in sera of patients diagnosed leptospirosis. Total protein and albumin were decreased in 18.5％ and 31.2％ of patients, respectively. AST, ALT, ALP, UN and creatinine were increased in 90.4％, 66.9％, 28.0％, 15.9％ and 10.8％ of patients, respectively. We performed cellulose acetate membrane electrophoresis (EP) on sera of patients increased both of AST and ALT, and of patients increased both of creatinine and UN. In patients increased both of AST and ALT, and in patients increased both of AST and ALT, the relative percentage of albumin to total protein in patient serum was dcreased in 89.1 ％ of patients. α₁-globulin, α₂-globulin, β-globulin and γ-globulin were increased in 85.1 ％, 75.2％, 33.6％ and 98.0％ of patients, respectively. In patients increased both of creatinine and UN, the relative percentage of albumin to total protein in patient serum was dcreased in 93.8％ of patients. α₁-globulin, α₂-globulin, β-globulin and γ-globulin were increased in 87.5％, 100％, 31.2％ and 93.8％ of patients, respectively. These data indicate that infection of Leptospira causes severe liver damage to most of leptospirosis patients, but doesn't cause renal damage to most of them. The relative rate of serum protein electrophoresis fractions to total protein are not identical with them of typical hepatitis patient.

• BMB Reports
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• v.28 no.2
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• pp.143-148
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• 1995

In E. coli, chromosomal DNA associated with proteins is condensed into an organized structure known as nucleoid. Using a nitrocellulose filter binding assay to identify proteins forming nucleoid, a 21 kDa protein was purified from E. coli. The molecular weight of the purified protein was 21 kDa on SDS-polyactylamide gel electrophoresis and 24 kDa on gel permeation chromatography. A molecular weight of 21 kDa on SDS-polyacrylamide gel electrophoresis is unique among known proteins which are believed to be involved in the formation of nucleoid in E. coli. The 21 kDa protein nonspecifically binds to both double-stranded and single-stranded DNA. Sedimentation in a sucrose gradient revealed that the protein induced significant condensation of both supercoiled plasmid DNA and linear bacteriophage $\lambda$ DNA On the basis of quantitative Western-blot analysis, approximately 40,000 molecules of the protein were estimated to exist in an E. coli. The biochemical properties and cellular abundance of the 21 kDa protein suggest that this protein participates in the formation of nucleoid in E. coli.

• Journal of Microbiology and Biotechnology
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• v.22 no.5
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• pp.654-658
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• 2012

Osteoarthritis (OA) is the most common rheumatic pathology. One of the major objectives of OA research is the development of early diagnostic strategies such as those using proteomic technology. Synovial fluid (SF) in OA patients is a potential source of biomarkers for OA. The efficient and reliable preparation of SF proteomes is a critical step towards biomarker discovery. In this study, we have optimized a pretreatment method for twodimensional gel electrophoresis (2DE) separation of the SF proteome, by enriching low-abundance proteins and simultaneously removing hyaluronic acid, albumin, and IgG. SF samples pretreated using this optimized method were then evaluated by 1DE and 2DE separation followed by immunodetection of cartilage oligomeric matrix protein (COMP), a known OA biomarker, and by the identification of 3 proteins (apolipoprotein, haptoglobin precursor, and fibrinogen D fragment) that are related to joint diseases.

• The Korean Journal of Zoology
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• v.8 no.2
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• pp.47-50
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• 1965

양서류 오종 Bombina orientalis , Cacopoides borealis , Bufo bufo asiaticus, Rana nigromaculata nigromaculata, Rana rugosa 의 혈청단백질을 Paper electrophoresis 의 방법으로 분석비교하였다. 그 결과 Bombina orientalis 의 혈청단백질은 인간의 것과 마찬가지로 5개의 protein fraction으로 나누어지고 그중 fraction III 단백지링 가장 많은 함량을 구성하며 peak 가 가장 높다. Cacopoides borealis 와 Bufo bufo asiaticus 의 혈청단백질은 4개의 protein fraction 으로 나누어지는데 Cacopoides boreealis 에서는 fraction IV protein이 Bufo bufo asiaticus 에서는 fraction I protein 이 가장 많은 함량을 구성하고 있다. Rana nigromaculata nigromacuata 와 Rana rugosa 는 graph 상에 나타난 peak로 보면 상호유사하나 protein fraction 수는 차이가 있다. 그리고 albumin은 전 함량 per centage의 약 반을 차지하고 있다. 즉 종간의 거리가 멀수록 protein fraction 의 차이가 percentage 함량에 있어서 명백하여짐을 암시하여준다.