• Korean Journal of Veterinary Research
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• v.31 no.3
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• pp.259-264
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• 1991

The proteins of the race horse erythrocyte membrane were analysed by polyacrylamide gel electrophoresis in sodium dodecyl sulfate(SDS-PAGE), and their relations to the fast erythrocyte sedimentation rate(ESR) of the race horse were investigated. The erythrocyte sedimentation rate of race horse were very fast compared with the human one(33 times <$90^{\circ}-plastic-ESR/30m$> and 25 times <$90^{\circ}-micro-ESR/30m$> as fast as the human one) are reported previously. Although the general protein profiles of the race horse erythrocyte membranes were almost similar to that of human, band 3 content was showing higher in race horse (34.7%) than in human (25.3%). The glycoprotein profiles of the race horse erythrocyte membranes revealed by periodic acid Schiff's(PAS) stain showed a marked difference from that of human. The PAS-1(glycophorin) and PAS-2(sialoglycoprotein) present in human erythrocyte memo brane were almost absent from the Holstein and race horse erythrocyte membranes, but PAS-2 was more in only race horse from that of human. Instead, the bovine erythrocyte membranes showed a strong PAS-B near the origin of the electrophorograms and the race horse erythrocyte membranes showed a strong PAS-negative band near the end of the electrophorograms, which is named as PAS-E in this study. These results suggest that the fast sedimentation rate of race horse erythrocyte is due in part to the presence of more band 3 protein fraction and PAS-E glycoproteins in the race horse erythrocytes.

• Journal of Microbiology
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• v.45 no.5
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• pp.402-408
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• 2007

A strain producing a potent protease was isolated from turban shell. The strain was identified as Bacillus sp. S17110 based on phylogenetic analysis. The enzyme was purified from culture supernatant of Bacillus sp. S17110 to homogeneity by ammonium sulfate precipitation, SP-Sepharose, and DEAE-Sepharose anion exchange chromatography. Protease activity of the purified protein against casein was found to be stable at pH 7 to pH 10 and around $50^{\circ}C$. Approximately 70% of proteolytic activity of the enzyme was detected either in the presence of 100 mM SDS or Tween 20. The enzyme activity was enhanced in the presence of $Ca^{2+},\;Zn^{2+},\;Mg^{2+}$, but was inhibited by EDTA, indicating that it requires metal for its activity. The purified enzyme was found to be a monomeric protein with a molecular mass of 75 kDa, as estimated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and gel filtration chromatography. The purified enzyme was analyzed through peptide fingerprint mass spectra generated from matrix-assisted laser desorption ionization-time-of-flight-mass spectrometry (MALDI-TOF-MS) and a BLAST search, and identified as immune inhibitor A (inhA) deduced from nucleotide sequence of B. cereus G9241. Since InhA was identified as protease that cleave antibacterial proteins found in insect, inhA-like protease purified from Bacillus sp. S17110 might be pathogenic to sea invertebrates.

• Food Science of Animal Resources
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• v.39 no.6
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• pp.1000-1007
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• 2019

This study investigated protein digestibility of beef puree in infant and adult in vitro digestion models. The simulated digestive juices for infant and adult were prepared. Protein digestibility of beef puree was calculated in the gastric and gastrointestinal compartments. The 10% trichloroacetic acid soluble nitrogen and α-amino group contents of gastric digesta were lower in the infant in vitro digestion model than those in the adult in vitro digestion model (p<0.05). In addition, the gastrointestinal digesta from the infant in vitro digestion model had lower value of the 10% trichloroacetic acid soluble nitrogen and α-amino group contents than those of the adult in vitro digestion model (p<0.05). The results of sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that the remarkable bands of actin and myosin light chain B were found in the digesta of beef puree from the infant in vitro digestion model. The results of this study revealed the lower protein digestibility of beef puree in infants compared to that in adults. Therefore, the development of ways to increase digestibility of meat protein can improve the nutritional quality of meat products for infants.

• Food Science of Animal Resources
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• v.39 no.6
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• pp.888-902
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• 2019

Our aim was to investigate the effects of bromelain embedded in double emulsion (DE) on physicochemical properties of pork loin. We evaluated DE characteristics such as size, zeta potential, and microscopy after fabrication. We marinated meat with distilled water (DW), 1% (w/v) bromelain solution, blank DE, and 1% (w/v) bromelain loaded in double emulsion (DE E) for 0, 24, 48, and 72 h at 4℃, and prepared raw meat for control. The marinated samples were assessed for color, water holding capacity, cooking loss, moisture content, pH, protein solubility, Warner-Bratzler shear force (WBSF) and gel electrophoresis. The droplet size of 1% (w/v) bromelain embedded in DE was increased compared with blank DE (p<0.05) and values of zeta potential decreased. The increase in lightness and color difference range of the DE-treated group was lower than that of the DW-treated group (p<0.05). Moreover, treatment by immersion in 1% (w/v) DE E resulted in the highest water holding capacity values (p<0.05) and lower cooking loss values than water base treatment (p<0.05). Results for myofibrillar protein solubility and WBSF showed a similar trend. 1% (w/v) DE E showed degradation of myosin heavy chain after 48 h in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Thus, bromelain-loaded DE is useful for controlling and handling enzyme activity in food industry.

• Korean Journal of Microbiology
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• v.31 no.1
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• pp.63-71
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• 1993

A xylanase (xylanase I) was purified 11.9-fold from the culture filtrate of Trichoderma koningii ATCC 26113 by the column chromatography on Sephadex G-75, SP-Sephadex C-50, DEAE-Sephadex A-50 and Sephadex G-50 with an overall yield of 8.2%. The molecular mass determined by gel filtration and sodium dodecyl sulfate polyacrylamide gel electrophoresis was found to be a monomeric polypeptide of ca. 35 kDa. The isoelectric point of the enzyme was estimated to be 9.3. The optimal reaction pH and temperature are 5.8 and 55.deg.C, respectively. The enzyme is stable up to 60.deg.C, while 78% of its activity is lost after the incubation for 10 min at 70.deg.C. The enzyme hydrolyzes sylan with relatively high activity, as well as carboxymethyl cellulose and avicel. The $K_{m}$ values of the enzyme for oat-spelf sylan, larchwood xylan and Avicel were 3.5, 1.6 and 10. 1 mg/ml, respectively. The enzyme hydrolyzed oat-spelt sylan to sylose, sylobiose, sylotriose and arabionoxylobiose, while it degraded larchwood xylan to xylose, xylobiose, xylotriose and arabionoxylobiose, while it degraded larchwood xylan to xylose, xylobiose and xylotriose as the major products. The hydrolysis patterns indicate that xylanase I is endo-enzyme.e.

• Journal of the Korean Society of Food Science and Nutrition
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• v.21 no.6
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• pp.712-718
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• 1992

This experiment was carried out to investigate some physico-chemical properties of myofibrillar proteins isolated from alkaline and acid rigor muscles of rabbit. The degree of fragmentation was about 0.35 at 3 days of postmortem in acid rigor muscle fiber, whereas it was only 0.3 at 7 days of postmortem in alkaline rigormuscle fiber. $Mg^{2+}$-activated ATPase activities of actomyosin were increased to the highest level at 1st day in acid rigor and at 3rd day in alkaline rigor muscle fiber. $Ca^{2+}$-activated ATPase activities of actomyosin were slightly increased at postmortem. $Mg^{2+}$-, and $Ca^{2+}$-activated ATPase activities were higher in alkaline rigor muscle than those in acid rigor muscle at postmortem. Solubility of actomyosin increased with postmortem but no differences were observed in rigor types. SDS-PAGE(sodium dodecyl sulfate polyacrylamide gel electrophoresis) band patterns of myofibrils did not show significant differences between rigor types, but newly 30.000 dalton proteins were appeared at 3 day postmortem in both rigor types.

• The Journal of Korean Medicine
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• v.26 no.1 s.61
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• pp.59-70
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• 2005

Objective: Tumor necrosis factor-a $(TNF-{\alpha})$, a potent immuno-modulator and pro-inflammatory cytokine, has been implicated in many pathological processes. In this study, the author examined whether promoter region polymorphism in the $TNF-{\alpha}$a gene at position-308 affect the odds of cerebral infarction (CI) and whether genetic risk is enhanced by sasang constitutional classification. Methods: 212 CI patients and 610 healthy controls were genotyped and determined according to sasang constitutional classification. The amplified genotypes were analyzed on $8\%$ polyacrylamide gel. The alleles were visualized by ethidium bromide staining. Primers for $TNF-{\alpha}$ were designed to incorporate a polymorphic site at a position -308 bp of the $TNF-{\alpha}$ gene into an NcoI restriction site. Restriction digests generated products of 87 and 20 bp for G allele and 107 bp for A allele. Results : A significant decrease was found for the $TNF-{\alpha}$ A allele in CI patients compared with controls (P=0.033, odds ratio, O.R.: 0.622). However, there was no significant association between $TNF-{\alpha}$ polymorphism and sasang constitution in CI patients. Conclusion: My finding suggests that $TNF-{\alpha}$promoter region polymorphism is responsible for susceptibility to CI in Koreans.

• Applied Biological Chemistry
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• v.29 no.1
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• pp.10-15
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• 1986

A polyacrylamide gel electrophoresis technique was applied to cytokinin-protein binding assay. Binding of soybean leaf proteins to cytokinin and relative affinities of protein fractions to cytokinin were studied. The electrophoresis technique appeared to be very useful for determination of cytokinin-protein binding, for identification of protein species binding to cytokinin and for comparison of relative affinities of the proteins to cytokinin. The presence of cytokinin-binding proteins in soybean leaves was confirmed from assays with ammonium sulfate precipitation, Sephadex G-25 chromatography, paper chromatography, and electrophoresis. Three groups of cytokinin-binding proteins were identified in the soybean leaf protein extract and two of the three showed low affinity to cytokinin, however, the third one with mobility between $0.0{\sim}0.2$, probably high molecular weight protein (s), showed high affinity in the electrophoretic analysis.

• Applied Biological Chemistry
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• v.29 no.3
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• pp.304-310
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• 1986

A. calcoaceticus C10 grown on cyclohexanol as sole source of carbon and energy produced cyclohexanol dehydrogenase(CDH) and glucose dehydrogenase (GDH) concomitantly. CDH and GDH were different in coenzyme, induction and electrophoretic patterns. CDH depended for activity on $NAD^+$ only, while GDH required $NAD^+$ or $NADP^+$ alternatively. CDH was produced in the medium added cyclohexanol, but GDH was produced in various media such as LB, LB added 0.2% glucose or cyclohexanol and cyclohexanol medium. Productivity of CDH in A. calcoaceticus C10 was enhanced about 8 times by the addition of 0.2% cyclohexanol to LB medium after 4 hours as much as LB medium only. Production of CDH was induced by cyclohexanol, cyclohexanone, cyclohexan-1,2-diol and cyclohexene oxide, but not induced by ${\varepsilon}-caprolactone$ and adipate.

• Microbiology and Biotechnology Letters
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• v.19 no.5
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• pp.470-476
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• 1991

The distribution of peroxidase activity in 9 kinds of cruciferous plants was investigated. Among the plants examined, peroxidase activity was found to be high levels in roots of Chinese cabbage. One kind of peroxidase was purified approximately 56-fold from crude extracts of Chinese cabbage roots. The molecular weight of the enzyme was 50, 000 and consisted oif a single polypeptide chain, as estimated by sodium dodecyl sulfate polyacrylamide gel electrophoresis and Sephadex G-150 gel column chromatography. The enzyme showed optimum activity at pH 7.0 and $50^{\circ}C$. Phenol and phenol derivatives serves as substrates of the enzyme and Km value for $H_2O_2$ was 1.6 mM toward pyrogallol. The enzyme showed a Soret band at 406 nm and this result indicate that the enzyme contained heme as a prosthetic group. The immunochemical and electrophoretic properties of purified peroxidase from Chinese cabbage were very similar to horseradish peroxidase.