• Journal of the East Asian Society of Dietary Life
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• v.16 no.6
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• pp.740-746
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• 2006

The proximates, vitamin C, minerals, and fatty acids of five potato cultivars were evaluated by AOAC methods, the hydrazine method, ICP-AES, and gas chromatography, respectively. The proximate analyses; vitamin C, reducing sugar, and soluble solid contents; and mineral and fatty acid compositions were significantly different among the five cultivars. The Superior cultivar contained a higher carbohydrate content and higher Ca/P ratio and lower levels of crude protein and Na. The Atlantic cultivar contained significantly higher amount of energy, carbohydrate, reducing sugar, vitamin C, SEA, and MUFA, and significantly lower amount of minerals and PUFA. The Shepody cultivar contained significantly higher amount of carbohydrate and MUFA, and significantly lower amount of soluble solid, vitamin C, and SFA. In addition, the P, Fe, Mg, Cu, and Al levels were significantly higher in Shepody, and Zn content was significantly lower. The Jopung cultivar contained significantly higher levels of moisture and Na, and significantly lower levels of soluble content, reducing sugar, carbohydrate, crude protein, and fat. Finally, the Namsuh cultivar contained significantly higher amount of soluble solid, crude protein, K, Mg, and Al, and significantly lower amount of reducing sugar.

• Biomedical Science Letters
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• v.6 no.3
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• pp.171-179
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• 2000

The lengths of thick and thin filaments in the sarcomeres of most vertebrate skeletal muscles are precisely regulated and are important structural parameters in understanding muscle contraction. Nebulin is a usually large protein that spans the whole length of thin filaments in the sarcomeres of skeletal muscles. In this paper we used SDS-PAGE and immunoblot to identify nebulin isoform proteins in muscle and non-muscle tissues. We prepared embryonic chicken tissues including skeletal muscle, cardiac muscle, smooth muscle, brain, liver to compare nebulin isoform proteins. The proteins were divided into soluble and insoluble fraction. As a result, we identified tissue specific expression of various nebulin isoform proteins in muscle and non-muscle tissues of chicken. Nebulin was detected in skeletal muscle of adult chicken about 500 kDa. Nebulett was expressed in cardiac muscle of embryonic and adult chicken about 107 kDa. A giant protein with molecular mass of about 380 kDa was identified in brain of non-muscle of chicken. This giant protein was detected in the soluble fraction of chicken embryo. The unequal distribution of the nebulin isoform proteins suggests tissue specific regulation of the isoform expression and indicates a functional specialization of the encoded isoform subtypes.

• Journal of Microbiology and Biotechnology
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• v.26 no.11
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• pp.1881-1890
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• 2016

Manganese superoxide dismutase (MnSOD) is a vital enzyme that protects cells from free radicals through eliminating superoxide radicals ($O^{2-}$). Hirudin, a kind of small active peptide molecule, is one of the strongest anticoagulants that can effectively cure thrombus diseases. In this study, we fused Hirudin to the C terminus of human MnSOD with the GGGGS linker to generate a novel dual-feature fusion protein, denoted as hMnSOD-Hirudin. The hMnSOD-Hirudin gene fragment was cloned into the pET15b (SmaI, CIAP) vector, forming a recombinant pET15b-hMnSOD-Hirudin plasmid, and then was transferred into Escherichia coli strain Rosetta-gami for expression. SDS-PAGE was used to detect the fusion protein, which was expected to be about 30 kDa upon IPTG induction. Furthermore, the hMnSOD-Hirudin protein was heavily detected as a soluble form in the supernatant. The purification rate observed after Ni NTA affinity chromatography was above 95%. The hMnSOD-Hirudin protein yield reached 67.25 mg per liter of bacterial culture. The identity of the purified protein was confirmed by western blotting. The hMnSOD-Hirudin protein activity assay evinced that the antioxidation activity of the hMnSOD-Hirudin protein obtained was $2,444.0{\pm}96.0U/mg$, and the anticoagulant activity of the hMnSOD-Hirudin protein was $599.0{\pm}35.0ATU/mg$. In addition, in vitro bioactivity assay showed that the hMnSOD-Hirudin protein had no or little cytotoxicity in H9c2, HK-2, and H9 (human $CD_4{^+}$, T cell) cell lines. Transwell migration assay and invasion assay showed that the hMnSOD-Hirudin protein could suppress human lung cancer 95-D cell metastasis and invasion in vitro.

• Food Engineering Progress
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• v.15 no.2
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• pp.143-147
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• 2011

For efficient extraction of protein from defatted rice bran, the 5 ranges of extraction pH (8, 9, 10, 11 and 12) and the 3 ranges of isoelectric precipitation pH (2, 4 and 6) were used. The protein content, browning reaction, the electrophoresis pattern and the recovery yield of soluble protein at each pH range were compared each other. The recovery yield of soluble protein increased in proportion to extraction pH, but at the same time, browning reaction became more conspicuous. The most amount of protein was recovered at the precipitation pH of 4. The SDS-PAGE patterns of the extracted proteins showed no significant correlations between pH and the protein content, but the highly alkaline condition was more advantageous to extract protein less than 35 kDa. In each pH range, the recovery yield of soluble protein averagely reached 32.5% on the basis of extraction. In result, it was found that combination of extraction pH 10 and precipitation pH 4, which resulted in 37.65% of recovery yield and low level of browning reaction, was the optimum condition for the extraction of protein from defatted rice bran.

• Journal of the Korean Society of Food Science and Nutrition
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• v.10 no.1
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• pp.85-91
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• 1981

The growing cells of S. aureus were fractionated along the Schmidt-Thannhauser-Schneider's technique into several fractions such as TCA(trichloroacetic acid)-soluble, lipid, nucleic acid, protein and residue fraction. They were also fractionated according to their cellular structure into Sonic-supernatant, SDS(sodium lauryl sulfate)-soluble, Formamide-soluble and Residue fraction. Fractionation was carried out by orderly treatment of the Sonic pellet with 1.0% SDS and hot$(150^{\circ}C)$ formamide, and the pellet was prepared by centrifugation of the cells sonic osillated for 20 minutes at 150 watt. Sonic-supernatant fraction contained a 91.3% of total DNA while other fractions contained less than 9.5%. SDS-soluble fraction showed a high activity of malate dehydrogenase(13.67 unit/mg protein) and which was higher 22.3 times than the activity found from unsoluble fraction. Formamide-soluble fraction prepared from SDS-undoluble pellet by using the hot formamide exhibited a clear action of reducing sugars against the Anthronesulfate, while it exhibited no clear action against the ninhydrin. However, contrastly, the residue remainnning after extraction with formamide exhibited a clear action against ninhydrin and glucosamine was detected form the hydrolysate of residue by paper chromatography. From these results it is considered that the Sonic-supernatant fraction is mainly consisted of plasmic component of the cells. Other fractions, SDS-soluble, Formamide-soluble and Residue, should be consisted of plasma membrane, lipoplysaccharide and peptidoglycan of the cell, respectively.

• Journal of the Korean Society of Food Science and Nutrition
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• v.26 no.2
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• pp.175-179
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• 1997

Changes of protein contents and chromatogram patterns by gel filtration chromatography was investigated for the purpose of studying changes of Proteins during softening of persimmon and jujube fruits. Contents of water-soluble and salt-soluble proteins were increased during softening of persimmon and jujube fruits, but that of cell wall-bound proteins was decreased. After performing a gel filtration of water-soluble protein, one peak was separated in mature persimmon fruits and three peaks in soft persimmon fruits. In the case of jujube fruits, there were three peaks in both of mature and soft fruits. Pattern of salt-soluble and cell wall-bound proteins by gel filtration chromatography hardly changed during softening. During softening of two fruits, the contents of water- soluble and salt-soluble proteins appeared to be increased on the same fractions with the decreasing in content of cell wall-bound proteins.

• 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.

• Proceedings of the SCSK Conference
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• 2003.09a
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• pp.142-160
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• 2003

Most consumers have noted hair damage following coloring treatments. Proper evaluation of hair bleaching products must be performed using quantitative assessments of hair damage, though they are difficult, because of the slight fluctuations in hair composition. In the present study, we utilized a sensitive evaluation method for hair damage and found that the amount of soluble protein fraction extracted from hair under a reducing condition, termed labile protein, dramatically increased after bleaching.(omitted)

• Korean Journal of Food Science and Technology
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• v.30 no.3
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• pp.557-561
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• 1998

This study was conducted to investigate the functionality of soybean protein isolates extracted in acidic range (pH 2.0 and 3.0), neutral range (pH 7.0) and alkaline range (pH 10.0 and 12.0). The protein content of soybean protein isolates extracted at pH 3.0 was maximum (93.31%), but that of pH 7.0 was minimum (73.93%). The extraction yield of soybean protein isolates extracted at pH 3.0 was minimum (0.36%), but that of pH 12.0 was maximum (47.54%). The functionality (solubility, water absorption, oil absorption, foam capacity, foam stability, emulsion capacity and gelation) of soybean protein isolates was significantly influenced by pH of extraction medium. The soybean protein isolates extracted at pH 2.0 and 3.0 were more soluble at acidic ranges and those of pH 3.0 and 7.0 were more soluble at neutral ranges, but those of pH 2.0, 3.0, 7.0, 10.0 and 12.0 were more soluble at alkaline ranges than other ranges. The soybean protein isolates extracted at pH 2.0 and pH 12.0 gave greater water absorption, oil absorption and foam capacity than those extracted at pH 3.0, pH 7.0 and pH 10.0. And the emulsion capacity of soybean protein isolates was increased by the increase of extraction pH.

• 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.