• Journal of the Korean Society of Clothing and Textiles
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• v.21 no.6
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• pp.970-976
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• 1997

Synthetic leather added collagen protein was coagulated in DMF solution. With increasing collagen concentration, thickness of synthetic leather increased. In addition, water vapor permeability and water vapor absoption increased with increasing collagen protein concentration. But MIU and SMD value of surface properties decreased with increasing collagen protein concentration. As a result, synthetic leather added collagen protein showed comfort and dry touch.

• Proceedings of the Korean Magnetic Resonance Society Conference
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• 2002.01a
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• pp.25-25
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• 2002

• Preventive Nutrition and Food Science
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• v.2 no.4
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• pp.328-332
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• 1997

The ripe fruit of Hass avocado contains one of the highest elvels of cytochrome P-450 protein found in the plant kingdom. To determine whether wounded roots of avocado contain P-450 protein, the roots of avocado were wounded by slicing, and then allowed to incubate in sealed plastic bags, in 0.4M mannitol, and in the solution to make protoplast preparation containing cellulysin and macerase during the specified times. The microsomal proteins were extracted from the samples, separated by SDS-PAGE, and then subjected to Western blot analysis using polyclonal antibodies which are generated against the CYP71A1 protein. wounded roots in sealed bags produced CYP71A1 within 6 hours after cutting, and those in 0.4M mannitol did not produce CYP71A1 even after 72 hours, but those in the protoplast preparation by cellulysin and macerase induced and produced CYP71A was induced in only 24 hours. These results indicate that CYP 71A1 plays a role for wound healing for root tissue o avocado, and would-inducible P-450 protein was not detected in the mannitol solution by preventing a synthesis of ethylene in a liquid state, but the softening of tissues by cellulysin and macerase to make protoplast preparation was involved in an activation of CYP 71A1 even in the liquid state.

• BMB Reports
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• v.31 no.4
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• pp.307-327
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• 1998

Cytochrome c peroxidase (CcP) is a yeast mitochondrial enzyme which catalyzes the reduction of hydrogen peroxide to water using two equivalents of ferrocytochrome c. The CcP/cytochrome c system has many features which make it a very useful model for detailed investigation of heme protein structure/function relationships including activation of hydrogen peroxide, protein-protein interactions, and long-range electron transfer. Both CcP and cytochrome c are single heme, single subunit proteins of modest size. High-resolution crystallographic structures of both proteins, of one-to-one complexes of the two proteins, and a number of active-site mutants are available. Site-directed mutagenesis studies indicate that the distal histidine in CcP is primarily responsible for rapid utilization of hydrogen peroxide implying significantly different properties of the distal histidine in the peroxidases compared to the globins. CcP and cytochrome c bind to form a dynamic one-to-one complex. The binding is largely electrostatic in nature with a small, unfavorable enthalpy of binding and a large positive entropy change upon complex formation. The cytochrome c-binding site on CcP has been mapped in solution by measuring the binding affinities between cytochrome c and a number of CcP surface mutations. The binding site for cytochrome c in solution is consistent with the crystallographic structure of the one-to-one complex. Evidence for the involvement of a second, low-affinity cytochrome c-binding site on CcP in long-range electron transfer between the two proteins is reviewed.

• BMB Reports
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• v.38 no.5
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• pp.550-554
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• 2005

YKR049C is a mitochondrial protein in Saccharomyces cerevisiae that is conserved among yeast species, including Candida albicans. However, no biological function for YKR049C has been ascribed based on its primary sequence information. In the present study, NMR spectroscopy was used to determine the putative biological function of YKR049C based on its solution structure. YKR049C shows a well-defined thioredoxin fold with a unique insertion of helices between two $\beta$-strands. The central $\beta$-sheet divides the protein into two parts; a unique face and a conserved face. The 'unique face' is located between ${\beta}2$ and ${\beta}3$. Interestingly, the sequences most conserved among YKR049C families are found on this 'unique face', which incorporates L109 to E114. The side chains of these conserved residues interact with residues on the helical region with a stretch of hydrophobic surface. A putative active site composed by two short helices and a single Cys97 was also well observed. Our findings suggest that YKR049C is a redox protein with a thioredoxin fold containing a single active cysteine.

• Korean Journal of Food Science and Technology
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• v.20 no.6
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• pp.840-844
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• 1988

High-protein rice flour (HPRF) was prepared by an enzymatic process using ${\alpha}-amylase$ and g1ucoamylase without cooking Process and the feasibility of HPRF as infants foods was tested. Rice flour slurry was treated with 0.25% ${\alpha}-amylase$ and 0.5% glucoamylase at $55^{\circ}C$ for 24hrs. After saccharification, the digested rice slurry was centrifuged and the precipitated paste, was then heat-dried to obtain HPRF. The protein content of the HPRF was 20.8%. On the other hand, the supernatant of glucose enriched solution was decolourized, deionized and then isomerised to furctose at $60^{\circ}C$ for 100min by using immobilized glucose isomerase column. The high-fructose solution (HFS) contained 56% glucose, 42% fructose and 2% oligosaccharide. The nutritional quality of the HPRF was compared with milk protein and soybean protein in weight gain, feed efficiency ratio (FER), protein efficiency ratio (PER) and liver weight. HPRF was almost the same in all items with milk and soybean protein, but significantly superior to rice flour group.

• Journal of Korean Ophthalmic Optics Society
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• v.15 no.3
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• pp.227-234
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• 2010

Purpose: The cleaning effect of protein deposit and the change of contact lens parameters by ultrasonic cleaner for eye glasses on the soft contact lenses were investigated. Methods: Etafilcon A contact lenses contaminated with protein, was ultrasonicated by ultrasonic cleaner for eye glasses and for the control group, spoiled contact lenses were cleaned by multi-purpose solution. The remaining protein deposits on the contact lenses were determined after extraction and the changes of overall diameter, base curve, center thickness power, and water contents on contact lenses were measured and surfaces of contact lenses were observed by scanning electron microscope. Results: The cleaning efficacies of multi-purpose solution on protein deposited etafilcon A contact lenses were 6.08%, and 23.73~33.92% in the group of ultrasonic cleaner for eye glasses with multi-purpose solution and 0~12.99% in the group of ultrasonic clear for contact lens with multipurpose solution depending on the treatment time. The changes of parameters and surface on contact lenses by ultrasonication were not observed. Conclusions: Ultrasonic cleaner for eye glasses can be used to eliminate protein deposits for the diagnostic soft contact lens in the office since it was effective to eliminate protein deposits and not caused change of parameters on soft contact lenses.

• Macromolecular Research
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• v.11 no.1
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• pp.53-61
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• 2003

A molecular-thermodynamic model is developed for the salt-induced protein precipitation. The protein molecules interact through four intermolecular potentials. An equation of state is derived based on the statistical mechanical perturbation theory with the modified Chiew's equation for the fluid phase, Young's equation for the solid phase as the reference system and a perturbation based on the protein-protein effective two body potential. The equation of state provides an expression for the chemical potential of the protein. In a single protein system, the phase separation is represented by fluid-fluid equilibria. The precipitation behaviors are simulated with the partition coefficient at various salt concentrations and degree of pre-aggregation effect for the protein particles. In a binary protein system, we regard the system as a fluid-solid phase equilibrium. At equilibrium, we compute the reduced osmotic pressure-composition diagram in the diverse protein size difference and salt concentrations.

• Applied Biological Chemistry
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• v.28 no.2
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• pp.88-91
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• 1985

For the systematic investigation of biochemical characteristics of Korean ginseng protein, protein fractions were analyzed by the techniques of sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. The effect of pH and various salts on extractibility of ginseng protein were determined while the amino acid composition was studied by amino acid autoanalyzer. The protein was consisted of 66.08% of albumin and 20.51% of glutelin. Extractability of ginseng protein was the lowest in pH 3.0 and the highest in $pH\;6.0{\sim}8.0$. Among the neutral salts solution, $0.4M\;Na_2CO_3$ showed maximum extractability while $1.0M\;MgSO_4$ solution showed the least extractability. Resonable precipitation was obtained by 40% of acetone and ammonium sulfate. It has been shown by SDS polyacrylamide gel electrophoresis that the soluble protein had 11 bands. The molecular weight for the main protein of the soluble protein wasestimated to be 43,000. In amino acid composition of water extracted protein, arginine content was the highest 47.17% while on the contray, proline and cystine contents were very low.

• KSBB Journal
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• v.6 no.1
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• pp.105-109
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• 1991

In separating alkaline protease from the bacteria (Bacillus licheniformis) fermentation broth using reverse micelle, effects of various factors;ionic strength, pH and surfactant concentration, on separation efficiency were studied. KCl controls the ionic strength. The lower KCl concentration was in the feed solution, the more protein and activity was recovered. The higher KCl concentration was in the stripping solution, the more protein and activity was recovered. Using sodium-di-2-ethylhexyl sulfosuccinate(Aerosol-OT or AOT) as a surfactant, the higher AOT concentration in the solvent, the more activity and protein were recovered. 0.1N NaOH and IN HCl were used to adjust pH. Maximum recovery of protein mass and activity were obtained at feed solution of pH 5.3. Maximum activity was recovered at stripping solution of pH 7.5