• Food Science and Biotechnology
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• v.18 no.6
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• pp.1330-1335
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• 2009

Although beneficial effects of dietary plant proteins on lipid metabolism are well documented, not much information exists on the influence of different seafood proteins on the lipid metabolism. The present study evaluated the effect of 2 marine proteins (tuna protein and scallop ovary proteins) in comparison to casein and soy protein in male Wistar rats. The concentration of total lipids in the plasma of rats fed experimental diets was significantly lower from that of control (278.2 mg/dL) group (p<0.05); and, the liver lipid content was not significantly different (p>0.05). Fecal excretion of cholesterol and bile acids was significantly higher in marine proteins and soy protein fed groups compared to casein only fed control (6.1 and 6.4 mg/day, respectively) group (p<0.05). No significant differences were observed in the mRNA concentrations of different transcriptional factors (p>0.05).

• Biomolecules & Therapeutics
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• v.2 no.2
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• pp.120-125
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• 1994

We obtained the total protein antibodies of Saccharomyces cerevisiae KCTC 1720 and Escherichia coli K-12 from the rabbit and the guinea pig to determine the host-derived proteins which may be remained in biotechnological products. The protein concentration of rabbit antibodies was 4.05 mg/mι in the case of yeast, 7.14 mg/mι in the case of E. coli and that of guinea pig antibodies was 1.90 mg/mι in the case of yeast, 7.17 mg/mι in the case of E. coli, respectively. To determine remained host-derived proteins in biotechnological products which produced by the hosts, S. cerevisiae or E. coli, we used a sandwich enzyme linked immunosorbent assay method in 96 well microplate. When the method applied to determine the remained host-derived proteins in commercial biotechnological products, it detected less than 3.5 ng/vial in human growth hormone, less than 1 ng/vial in hepatitis B vaccine and interferon-${\gamma}$ and 2~23 ng/vial in interferon-$\alpha$. The method can be used to determine the remained host-derived protein in biotechnological products.

• Mass Spectrometry Letters
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• v.11 no.3
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• pp.52-58
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• 2020

Histidine phosphorylation (pHis) is increasingly recognized as an important post translational modification (PTM) in regulating cellular functions in eukaryotes. In order to clarify the role of pHis in mammalian cell signaling system, a global phosphorylation study was performed in human prostate cancer cells, PC-3M, using a TiO₂ affinity chromatography. A total number of 307 pHis sites were identified on the 268 proteins among total identified 9,924 phosphorylation sites on 3,316 proteins. In addition, 22 pHis proteins were classified in enzyme category. This report provides the first database for the study of pHis in prostate cancer cells.

• Journal of Microbiology
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• v.38 no.1
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• pp.1-7
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• 2000

Eight strains of Aeromonas hydrophila isolated from diseased trout in Korea were characterized and compared with an American type strain by various methods including biochemical and physiological tests, PCR, randomly amplified polymorphic DNA (RAPD), plasmid profiling, and gel electrophoresis of total, membrane, and extracellular proteins. Virulence factors such as surface array proteins, cytotoxin, hemolysin, haemagglutinin, and protease were also investigated. The Korean strains showed heterogeneity in Iysine decarboxylase production, utilization of various carbon sources, and production of acetoin. Five strains had the same profiles of total and membrane proteins. Six strains haemagglutinated with trout red blood cells (RBCs) which was inhibited by fucose, galactose, and mannose, except for No. 1 where haemagglutination was inhibited by only galactose and mannose, but not by fucose. Four isolates haemagglutinated with human RBCs which was inhibited by fucose and mannose yet not by galactose. The type strain haemagglutinated only with trout RBCs which was inhibited by fucose, galactose, and mannose. Every isolate secreted protease, hemolysin, cytotoxin, and siderophore, but no enterotoxin. Results showed that the Korean isolates, except for No.7, had very different biochemical and molecular characteristics from those of the American type strain.

• Korean Journal of Veterinary Research
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• v.31 no.1
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• pp.99-108
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• 1991

To observe the changes of serum proteins according to the process of Babesia gibsoni(B gibsoni) infection, the babesia protozoa($10^8/kg$) were inoculated into the cephalic vein of healthy dogs. The serum proteins of experimentally infected dogs were separated by using cellulose acetate electrophoresis. The results obtained were as follows; 1. Cellulose acetate electrophoresis was fractionated to total 6 of bands such as, albumin, ${\alpha}_1$, ${\alpha}_2$, ${\beta}_1$, ${\beta}_2$ and $\gamma$-globulin. 2. The concentration of total protein was shown a decreasing tendency after B gibsoni infection. Albumin and A/G ratio were lowered through all periods of the infection, but they were not significant changes. 3. The level of ${\alpha}_1$-globulin was significantly(p<0.05) incresed in early stage of the infection. 4. The levels of ${\alpha}_2$ and total $\alpha$-globulin were shown highly significant decreases (p<0.01) through all periods of the infection. 5. The levels of ${\beta}_1$ and total $\beta$-globulin had highly significant changes (p<0.01) that was increased in early stage of infection and decreased later. 6. The level of $\gamma$-globulin was seen to be constantly increased through all periods of infection. It was a highly significant change (p<0.01). 7. Plasma protein: fibrinogen (PP:F) ratio was shown a temporally significant increase (p<0.05) following the decrease in early infection.

• The Korean Journal of Ecology
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• v.21 no.6
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• pp.771-777
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• 1998

Aqueous extracts of Pinus rigida changed the electrophoretic patterns of total proteins and of hydrolytic enzymes such as peroxidase, esterase and amylase during the germination of radish (Raphanus sativus var. hortensis for. acanthiformis). When the extract treatment was finished, at the late stage of radish germination, aqueous extracts of P. rigida had suppressed the expression of 24 KD and 60 KD proteins. the extract induced new isozyme bands, indicating concomitant activity of peroxidases, esterase activities were stimulated in the cathodic region. The activity of amylase was enhanced by the extract.

• Korean Journal of Microbiology
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• v.31 no.2
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• pp.166-174
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• 1993

Streptomyces coeUc%r (Muller) cells were treated with $100 \mu$M hydrogen peroxide for I hour and proteins synthesized during hydrogen peroxide stress were labeled with L-[$^{35}S$]-methionine. Total cellular proteins were extracted and analyzed by two-dimensional polyacrylamide gel electrophoresis. In exponential growth phase, synthesis of about 100 proteins was increased by hydrogen peroxide treatment. These proteins were named as Pin (£eroxide-inducib]e) proteins and classified into 4 subgroups according to their induction time after hydrogen peroxide treatment. About 60 of them were found to be induced within 20 minutes and maintained throughout I hour of treatment. In stationary growth phase. synthesis of 62 proteins was increased by hydrogen peroxide and 21 of them were the same Pins found in exponential growth phase. Proteins from the mutants which are resistant to hydrogen peroxide were obtained in exponential growth phase and compared with those from the wild type on two-dimensional gel. The three mutants, N7, N9. and N24, were found to have higher constitutive leve]s of ]5, 17, and 15 Pin proteins respectively, than the wild type. 9 of these Pin proteins (D74.7a, E76.0c, E23.3. F50.7, F47.2a. F25.5, G39.6b, G24.0, H39.6a) increased in two of the three mutants and 3 proteins (F39.7, H6I.7. 120.8) increased in all of the three mutants. These proteins might play important roles in the response of S. coelic%r to hydrogen peroxide.

• Journal of Animal Science and Technology
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• v.57 no.12
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• pp.44.1-44.9
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• 2015

Background: Heat shock proteins play an important role in protection from stress stimuli and metabolic insults in almost all organisms. Methods: In this study, computational tools were used to deeply analyse the physicochemical characteristics and, using homology modelling, reliably predict the tertiary structure of the blunt snout bream (Ma-) Hsp70 and Hsc70 proteins. Derived three-dimensional models were then used to predict the function of the proteins. Results: Previously published predictions regarding the protein length, molecular weight, theoretical isoelectric point and total number of positive and negative residues were corroborated. Among the new findings are: the extinction coefficient (33725/33350 and 35090/34840 - Ma-Hsp70/ Ma-Hsc70, respectively), instability index (33.68/35.56 - both stable), aliphatic index (83.44/80.23 - both very stable), half-life estimates (both relatively stable), grand average of hydropathicity (-0.431/-0.473 - both hydrophilic) and amino acid composition (alanine-lysine-glycine/glycine-lysine-aspartic acid were the most abundant, no disulphide bonds, the N-terminal of both proteins was methionine). Homology modelling was performed by SWISS-MODEL program and the proposed model was evaluated as highly reliable based on PROCHECK's Ramachandran plot, ERRAT, PROVE, Verify 3D, ProQ and ProSA analyses. Conclusions: The research revealed a high structural similarity to Hsp70 and Hsc70 proteins from several taxonomically distant animal species, corroborating a remarkably high level of evolutionary conservation among the members of this protein family. Functional annotation based on structural similarity provides a reliable additional indirect evidence for a high level of functional conservation of these two genes/proteins in blunt snout bream, but it is not sensitive enough to functionally distinguish the two isoforms.

• Asian-Australasian Journal of Animal Sciences
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• v.24 no.9
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• pp.1288-1302
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• 2011

The aim of this study was to analyze the proteome expression of bovine satellite cells from longissimus dorsi (LD), deep pectoral (DP) and semitendinosus (ST) muscle depots during in vitro myogenic differentiation. Proteomic profiling by twodimensional gel electrophoresis and mass spectrometry of differentiating satellite cells revealed a total of 38 proteins that were differentially regulated among the three depots. Among differentially regulated proteins, metabolic proteins like lactate dehydrogenase (LDH), malate dehydrogenase (MDH) were found to be up regulated in ST, while alpha-enolase (NNE) in LD and DP depot satellite cells were down regulated. Also, our analysis found that there was a prominent up regulation of cytoskeletal proteins like actin, actincapping protein and transgelin along with chaperone proteins like heat shock protein beta 1 (HSPB 1) and T-complex protein 1 (TCP-1). Among other up regulated proteins, LIM domain containing protein, annexin 2 and Rho GDP-dissociation inhibitor 1 (Rho GDI) are observed, which were already proven to be involved in the myogeneis. More interestingly, satellite cells from ST depot were found to have a higher myotube formation rate than the cells from the other two depots. Taken together, our results demonstrated that, proteins involved in glucose metabolism, cytoskeletal modeling and protein folding plays a key role in the myogenic differentiation of bovine satellite cells.

• Journal of Korean Biological Nursing Science
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• v.22 no.2
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• pp.119-126
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• 2020

Purpose:Weight gain after kidney transplantation is a critical factor that can lead to poor outcomes with cardiovascular complications. Many studies have been conducted to identify predictive markers of future weight changes at the time of transplant. Recently, circulating exosomes and its contents including miRNAs and proteins have attracted attention as potential biomarkers. In this pilot study, we investigated exosomal proteins and weight change after kidney transplant. Methods: Recipients (n = 10) were classified into two groups; weight gainers (n = 5, 9.7 ± 4.4kg) and weight losers (n = 5, -6.4 ± 1.8kg) based on their weight changes at 12-months posttransplant. Based on the exosomal protein profiles obtained by the LC-MS/MS, differentially expressed proteins were identified between the groups. Results: Concentration and the mean size of exosomes significantly increased at 12-months compared to the baseline (p= .009) in the total group. Eleven exosomal proteins were found at the baseline as differentially expressed between the two groups. In the weight gain group, complement proteins including HV169, C3, C4B, and C4A, were significantly upregulated. Conclusion: Our pilot study suggests that exosomal complementary proteins are associated with weight gain after kidney transplantation. Further studies are needed to clarify the role of these exosomal proteins in the underlying mechanisms of weight changes in kidney transplant recipients.