• The Korean Journal of Zoology
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• v.33 no.2
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• pp.191-199
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• 1990

Sarcoplasmic reticulum subfractions were isolated from rabbit sarcoplasmic reticulum vesicles using ultracentrifugation in a continuous sucrose gradient (12.5% 50%) after French pressure treatment. And proteins in sarcoplasmic reticulum were detected by SDS-polyacrylamide gel electrophoresis and glycoproteins were identified through the reaction with 1251-concanavalin A.The electrophoresis showed that sarcoplasmic reticulum contained predominantly $Ca^2$+-AThase and calsequestrin along with high affinity calcium binding protein, intrinsic glycoprotein 160 Kd, 94 Kd, 80 Kd, 38 Kd, 34 Kd and 24 Kd proteins. Among these, the protein of about 80 Kd which has been known as one of heat shock proteins was especially enriched in the terminal cistemae of sarcoplasmic reticulum. Meanwhile, autoradiogram of 125 I-concanavalin A bound to the stained gels showed the distribution of glycoproteins which included 160 Kd glycoprotein, 94 Kd glycoprotein, calsequestrin and intrinsic glycoprotein Among these, the protein of about 160 Kd was especially enriched in longitudial sarcoplasmic reticulum and T-tubule, and the protein of about 94 Kd which has been known as one of glucose-regulated proteins was also enriched in T-tubule and sharply reduced in terminal cistemae.

• Journal of Animal Science and Technology
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• v.63 no.2
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• pp.417-425
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• 2021

The use of edible insects to replace meat protein is important to ensure future global food security. However, processed foods using edible insects require development to enhance consumer perception. Here, we examined the physicochemical characteristics and rheological properties of emulsions prepared from different edible insect larvae. Three edible insect species (Tenebrio molitor, Allomyrina dichotoma and Protaetia brevitarsis seulensis) were used to prepare larval emulsions that were formulated with 65% of insect larvae, 20% of pork back fat, and 15% ice. The A. dichotoma emulsion had the highest pH and lightness, redness, and yellowness values, while the T. molitor emulsion had the lowest pH and lightness, redness, and yellowness values. The T. molitor emulsion had the highest hardness, gumminess, chewiness, and apparent viscosity values but the lowest springiness and cohesiveness values. According to the sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis, T. molitor had the thickest bands, followed by P. brevitarsis seulensis. The differential scanning calorimetry distributions for the T. molitor and A. dichotoma emulsions showed one peak, while that of the P. brevitarsis seulensis emulsion had two peaks. The collective results suggest that T. molitor was the most suitable candidate (of the three tested species) for use as a meat replacement in terms of its physicochemical and rheological properties. It is important that such properties of insect-based emulsions are maintained using various technologies.

• Microbiology and Biotechnology Letters
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• v.17 no.4
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• pp.385-391
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• 1989

D-Glucose isomerase (D-xylose ketol isomerase, EC 5.3.1.5) was purified from the Alkalophilic Bacillus sp. No. 1911 by ammonium sulfate precipitation, DEAE-cellulose ion exchange chromatography followed by Sephadex G-150 gel filtration chromatography. Molecular weight of the purified enzyme was estimated to be 11, 000 by gel filtration on Sephadex G-200, and SDS-polyacrylamide gel electrophoresis showed that the enzyme consisted of four identical or similar subunits with a molecular weight of 43, 000. The enzyme was the most active at pH 7.5 and $65^{\circ}C$, and stable up to 7$0^{\circ}C$ at pH 7.5 and in the range of pH 6-9 at 6$0^{\circ}C$ by 30 min incubation in the presence of Co$^{++}$.

• Korean journal of applied entomology
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• v.34 no.2
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• pp.140-146
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• 1995

Changes in protein content during oocyte development was measured and egg-specific protein was characterized from the eggs in Lucilia illustris. During normal development ovarian protein was rapidly increased at 72hr and reached maximum at 96hr after a protein meal, when the eggs were fully matured. Purified protein from the ovaries by gel filtration of DEAE-cellulose an Sephacryl S-200 was loaded on 7.5% native polyacrylamide gel electrophoresis and identified at ${R}_{f}$ 0.4 as egg-specific protein, which has a mol. wt of 110,000. A total of 13 amino acids in th egg-specific protein was identified and expecially asparagine, glutamic acid, and tyrosine were highly concentrated. Five fatty acids were also identified. It is suggested that there is a specific protein in the eggs of L. illustris except yolk protein synthesized and secreted by fat body.

• Journal of Microbiology and Biotechnology
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• v.20 no.3
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• pp.558-562
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• 2010

SDS-PAGE of extracted surface-associated proteins of Lactobacillus rhamnosus strains E/N, Oxy, and Pen, was performed. The obtained protein patterns allowed differentiation of the examined strains, which was not accomplished by the commonly used RAPD genotypic method. The differentiation by the SDS-PAGE method proved to be a useful tool for strain-specific identification, which was further confirmed by 2DE analysis. Therefore, it can be used as an alternative or complementary method for both conventional and genotypic identification procedures, especially when closely related lactobacilli isolates are identified.

• Korean Journal of Microbiology
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• v.27 no.1
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• pp.27-34
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• 1989

In order to evaluate the applicability of enzyme electrophoresis for the identification of intra/interspecific hybride obtained by the protoplast fusion in Trichoderma, soluble proteins, intracellular soluble enzymes and extracellular $\beta$-glucosidase were analyzed by polyacrylamide gel electrophorsis. As the results, patterns of soluble protein, and isozyme patterns of peroxidase, malate dehydrogenase, and $\beta$-glucosidase in hydrids were defferent from those in parental and wild type strains. Therefore, it was established that the analysis of protein pattern by electrophoresis could be applied to isolate and identify the hybrids from the protoplast fusion.

• Preventive Nutrition and Food Science
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• v.7 no.1
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• pp.48-51
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• 2002

In order to study the reaction behavior of bovine holo- and apo-$\alpha$-lactalbumin ($\alpha$-La) during heat treatment at 65~10$0^{\circ}C$, the samples were analysed by first (ID)-and second-dimensional (2D) native-polyacrylamide gel electrophoresis (Native-PAGE) and sodium dodecylsulfate (SDS)-PAGE. When bolo-$\alpha$-La or apo- $\alpha$ -La were heated, they formed non-native, monomers, dimers and trimers. The apo-$\alpha$-La was more heat-sensitive than holo-$\alpha$-La. The monomers seemed to have the same composition as the native $\alpha$-La, but many of the disulfide bonds could be non-native.

• Journal of Microbiology and Biotechnology
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• v.6 no.5
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• pp.361-363
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• 1996

The terminal regions of the double-stranded RNA (dsRNA) genome segments of infectious pancreatic necrosis virus (IPNV) DRT strain were sequenced. The dsRNAs, which were $^{32}P$-labelled at their 3'-termini by incubation with [$^{32}P$]pCp and T4 RNA ligase, were separated by 5$%$ polyacrylamide gel electrophoresis, and the segments A and B of IPNV-DRT were sequenced by two-dimensional gel electrophoresis. The 5'-terminal sequences of the IPNV-DRT plus strand from two genome segments were found to have the same conserved nucleotide (5'-CGG(C/A)A-), but the 3'-terminal sequences -CCCCAGGCG-3' and -CGGACCCCG-3' were found in the plus strand from segments A and B, respectively. The inverted oligonucleotide sequences of 3'-terminal of between segments A and B were found and they differ from those of other IPNVs.

• Food Science of Animal Resources
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• v.34 no.5
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• pp.656-664
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• 2014

The purpose of this study was to analyze myosin heavy chain (MHC) isoforms in bovine longissimus thoracis (LT) muscle by liquid chromatography (LC) and mass spectrometry (MS). LT muscles taken from Hanwoo (Korean native cattle) steer (n=3) used to separate myosin bands by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The peptide queries were obtained from the myosin bands by LC-MS/MS analysis following in-gel digestion with trypsin. A total of 33 and 43 queries were identified as common and unique peptides, respectively, of MHC isoforms (individual ions scores >43 indicate identity or extensive homology, p<0.05). MHC-1 (IIx), -2 (IIa), -4 (IIb), and -7 (slow/I) were identified based on the Mowse score (5118, 3951, 2526, and 2541 for MHC-1, -2, -4, and -7, respectively). However, more analysis is needed to confirm the expression of MHC-4 in bovine LT muscle because any query identified as a unique peptide of MHC-4 was not found. The queries that were identified as unique peptides could be used as peptide markers to confirm MHC-1 (14 queries), -2 (8 queries), and -7 (21 queries) in bovine LT muscle; no query identified as a unique peptide of MHC-4 was found. LC-MS/MS analysis is a useful approach to study MHC isoforms at the protein level.

• Korean Journal of Acupuncture
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• v.37 no.2
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• pp.88-96
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• 2020

Objectives : The purpose of this study was to investigate the anti-oxidant and anti-aging effect of the seed of Euphorbia lathyris L. extracted by supercritical CO₂. Methods : Human dermal fibroblast cells dosed with the extract from Euphorbia lathyris L. were harvested and the intracellular proteome was analyzed to examine the expression of proteins related collagen synthesis pathway, metalloproteinases (MMPs), extracellular matrix (ECM)-cell interaction, cytokines, and antioxidant enzymes by 2-dimensional gel electrophoresis. Results : Fatty acid analysis of the extract from Euphorbia lathyris L. showed oleic acid was 84% and linoleic acid was 4.1%. Antioxidative effect was about 53% by beta carotene bleaching assay. In 2-dimensional polyacrylamide gel electrophoresis (2-D PAGE) analysis, fifteen protein changes in five mechanisms which were collagen synthesis pathway, MMPs, ECM-cell interaction, cytokines, and antioxidant enzymes were analyzed. Conclusions : This study suggests the supercritical extraction from the seed of Euphorbia lathyris L. could be used as anti-oxidant substances for pharmacopuncture.