• Journal of Life Science
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• v.18 no.8
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• pp.1036-1041
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• 2008

Methenyltetrahydrofolate synthetase extract was obtained from mouse liver and purified via $30{\sim}70%$ ammonium sulfate fractionation, Fast Q anion exchange and phenyl agarose chromatography. HPLC gel chromatography and SDS-polyacrylamide electrophoresis experiments showed that the enzyme is a monomer with molecular weight of 23 kDa. Optimum temperature and pH were $35^{\circ}C$ and 6.5, respectively. The enzyme was chemically modified only by tetranitromethane and 1-ethyl-3- (3-dimethyl aminopropyl)-carbodiimide (EDC), indicating that tyrosine and carboxylate are in the active site. pH studies showed that 2 tyrosines are involved in the binding of the substrates and a carboxylate in catalysis. Therefore, the chemical mechanism of the enzyme is likely that 2 tyrosines bind to ATP and 5-formylTHFand a carboxylate acts as a general base.

• Applied Biological Chemistry
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• v.27 no.2
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• pp.129-134
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• 1984

Change of protein component in soybean sprout grown at four temperatures was investigated by polyacrylamide gel electrophoresis. Main bands were identified using purified seed globulins. Electrophoretogram showed 5 main bands (a. b, c, d, and p) and 10 minor bands in seed and maximum number (19) of bands (8 main band including 0 and 11 minor) at 4th day after germination in cotyledon. All bands appeared in axis protein but resolution was poor. In cotyledon, a component (most rapidly) and b+c+d component decreased while o+p component and other minor components were increased at 6th day and decreased thereafter. In axis all components increased rapidly, especially in minor components and b+c+d component. High growing temperature accelerated decrease in cotyledon and increase in axis of protein, especially for 11S. The a component was identified as 7S, b+c+d as 11S and o+p as 2S globulin.

• Applied Biological Chemistry
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• v.35 no.3
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• pp.173-178
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• 1992

A bacterium having CMCase activity was isolated form soil and identifed as a Pseudomonas sp YD-15. The optimum conditions for the production of CMCase were avicel 1.2%, yeast extract 0.5%, $KNO_3$ 0.06%, $K_2HPO_4$ 0.2%, $MgSO_4$ $7H_2O$ 0.15%, pH 8.0, $30^{\circ}C$ and 60 hours cultivation. The CMCase was purified 15.2 folds with 14ft yield through ammonium sulfate precipitation, DEAE-sepharose column chromatography and sephadex G-100 gel filtration chromatography. The optimum pH and temperature for the enzyme activity were 6.0 and $50^{\circ}C$, respectively. The enzyme was stable between pH 5.0 and 8.0, below $50^{\circ}C$. The molecular weight was calculated about 100,000 by SDS-polyacrylamide gel electrophoresis. $K_m$ value for CMC used as a substrate was 40 mg/ml.

• Journal of the Korean Society of Food Science and Nutrition
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• v.16 no.4
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• pp.306-310
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• 1987

These experiments were conducted to find out the possibility of utilizing apricot seed as resources of food protein. The apricot seed contained 23.3% of crude protein. The salt soluble protein of apricot seed was highly dispersible in 0.2M sodium phosphate buffer containing about 0.3M $MgSO_4$, and the extractability of seed protein was about 35%. Major amino acid composition of apricot protein were glutamic acid and aspartic acid. The electrophoretic analysis showed 9 bands in apricot seed protein. Molecular weight for the main protein of the apricot seed separated by 1% SDS polyacrylamide gel electrophoresis was 49,000. Molecular weights of salt soluble protein measured by Sephadex G-200 was 110,000.

• BMB Reports
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• v.29 no.3
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• pp.253-260
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• 1996

An enzyme that hydrolyzes flavin-adenine dinucleotide (FAD) was found to be present in rat liver lysosomal membrane prepared from Triton WR-1339 filled lysosomes (tritosomes) purified by flotation on sucrose. This FAD phosphohydrolase (FADase) exhibited optimal activity at pH 8.5 and had an apparent Km of approximately 3.3 mM. The activity was decreased 50~70% by dialysis against EDTA and this was restored by $Zn^{2+}$, $Mg^{+2}$, $Hg^{+2}$, and $Ca^{+2}$ ions inhibited the enzyme, but $F^-$ and molybdate had no effect. The enzyme was also inhibited by p-chloromercuribenzoate (pCMB), reduced glutathione and other thiols, cyanide, and ascorbate. The presence of ATP, ADP, AMP. ${\alpha}-{\beta}-methylene$ ATP, AMP-p-nitrophenyl phosphate (PNP), GMP, and coenzyme A (CoA) decreased the activity on FAD, but pyrimidine nucleotides, adenosine, adenine, or $NAD^+$ were without effect. Phosphate stimulated the activity slightly. FAD phosphohydrolase activity was separated from ATPase and inorganic pyrophosphatase activities by solubilization with detergents and polyacrylamide gel electrophoresis and by linear sucrose density gradient centrifugation suggesting that the enzyme is different from ATPase, inorganic pyrophosphatase, and soluble lysosomal FAD pyrophosphatase. Paper chromatography showed that FAD was hydrolyzed to flavin mononucleotide (FMN) and AMP which were further hydrolyzed to riboflavin and AMP by phosphatases known to be present in lysosomal membranes. Incubation of the intact Iysosomes with pronase showed that the active site of FAD phosphohydrolase must be oriented to the cytosol. The FAD hydrolyzing activity was detected in Golgi, microsome, and plasma membrane, but not in mitochondria or soluble lysosomal preparations.

• Transactions of the Korean Society of Mechanical Engineers
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• v.14 no.1
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• pp.241-250
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• 1990

Characteristic relaxation time and characteristic diffusion time of viscoelastic fluids are determined experimentally by measuring the zero-shear-rate viscosity by falling ball viscometer and the infinite-shear-rate viscosity by capillary tube viscometer. Fluids used in experiments are aqueous solutions of polyacrylamide Separan AP-273 and the polymer concentrations range from 300 to 2000 wppm. A newly designed laser beam and timer system is employed to overcome the difficulty in measuring terminal velocities of the low concentration solutions. Ball removal device is prepared to remove the dropped ball from the bottom of cylinder without disturbing the testing fluid. In order to measure the zero-shear-rate viscosity, densities of hollow aluminium balls are adjusted very close to the densities of testing fluids. Characteristic diffusion time, which is ball viscometer. However, terminal velocity of a needle by falling ball viscometer is not affected by the time interval of dropping needles and characteristic diffusion time is not measured with a dropping needle. Powell-Eyring model predicts the highest values of the characteristic relaxation times among models used for heat transfer experimental works for a given polymer solution. As degradation of a polymer solution continues, the zero-shear-rate viscosity decreases more seriously than the infinite-shear-rate viscosity. Characteristic relaxation times of polymer solutions decreases as degradation continues.

• Korean Journal of Animal Reproduction
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• v.19 no.3
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• pp.235-241
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• 1995

These experiments were carried out to find genetic polymorphisms of Serum protein like Pre-albumin(Pr), Albumin(Al) and Transferrin(Tf), and establish preservation of pure pedigree in Korean Native Goats(KNG). Their serum was collected and examined from the total of 74 KNG that raised in Tang Jin district, Chungnam-province. They were biochemically analysed by polyacrylamide gel(7.5%) electrophoresis(PAGE) in order to estimate the frequencies of genotypes and alleles existing on each trait locus. The results obtained in these experiments were summarized as follows ; 1. In the serum Pre-albumin(Pr) locus, the frequencies of genotypes for hetero AB and homo BB observed were 55.4%, and 44.6%, respectively. While homo AA was not found in the Pr locus. The frequencies of gene in PrA and PrB were 0.723 and 0.277, respectively. Accordingly, the Pr loci were assumed to be controlled by alleles PrA and PrB. 2. The frequencies of genotypes of homo BB and hetero AB detected in Albumin(Al) locus were 75.7% and 24.3%, respectively. However, AA type was not observed in the Al locus. The gene frequencies of AlA an AlB were 0.879 and 0.121, respectively. Also, the Al loci were considered to be controlled by alleles AlA and AlB. 3. The frequencies of genotypes for hetero AD and homo DD found in Transferrin (Al) locus were 79.7% and 20.3%, respectively. Whereas, homotype AA was not detected in this locus. The gene frequencies of TfA and TfD were 0.399 and 0.601, respectively. Therefore, the serum Tf loci were assumed to be controlled by alleles Tfa and Tfd.

• Food Science of Animal Resources
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• v.38 no.2
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• pp.291-301
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• 2018

To shorten the production cycle of Zaodan, this study first pickled Zaodan by a novel technology - vacuum decompression technology. Vacuum decompression technology could reduce the pickling time of Zaodan from 20 wk to about 9 wk. The protein content, moisture and pH of the Zaodan egg white gradually decreased with a concomitant increase in salt during the pickling process. The total sulfhydryl group (SH) group content of the egg white proteins was increased to $2.43{\times}10^{-3}mol/L$ after being pickled for 30 d, whereas the content of disulphide bonds (SS) was reduced to $23.35{\times}10^{-3}mol/L$. The surface hydrophobicity was lowest after pickling for 30 d. In addition, great changes occurred in the secondary structure of the egg white proteins after pickling for 20 d. The disappearance of ovomucin was noticeable based on sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis.

• Korean Journal of Food Science and Technology
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• v.18 no.5
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• pp.339-344
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• 1986

The specific reaction of trypsin inhibitors with trypsin to form stable complexes was successfully applied for detection of trypsin inhibitors in soybean. Soybean extract was treated with $Ca^{++}$ to remove globulin fraction, followed by digestion with trypsin and fractionated by chromatography on Sephadex G-50. The void volume fraction contained the trypsin-trypsin inhibitor complexes as well as trypsin. The trypsin inhibitors were then detected by their molecular weight differences on SDS-polyacrylamide gel electrophoresis, in which the complexes dissociate into trypsin and its inhibitors. With the method proposed, trypsin inhibitors were indentified by their ability forming the stable complexes with trypsin and their anti-tryptic moiety. The formation of the complexes with trypsin was further confirmed by two dimensional electrophoresis and DEAE-Sephadex A-25 chromatography. Employing the proposed method, it was found that soybean (Glycine max cv. Hill) contained 7 trypsin inhibitors.

• Korean Journal of Food Science and Technology
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• v.20 no.1
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• pp.34-39
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• 1988

The possibility of using sodium dodecylsulfate-polyacrylamide gel electrophoresis was studied to detect specific proteins and their content in meat products such as beef, pork, fish, soybean, fish paste, ham and fish sausage. Many complicated bands were observed in the total protein fractions of the tested samples. The number of protein bands in the low salt-soluble protein fractions was considerably lesser and showed more specific bands in comparison with total protein fractions. Actone-insoluble fractions of non-meat proteins showed different patterns from meat proteins. A heating procedure seemed to be a cause for the diminished number and quantity of resolved protein bands in sausages. The results suggest that the discgel electrophoresis can be used to detect specific proteins and their content in protein foods, if a selective extraction method is emplyed.