• The Korean Journal of Community Living Science
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• v.16 no.4
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• pp.39-45
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• 2005

The aim of this study is to investigate the effects of hot water soluble extract from green tea on the components of serum and the liver and the antioxidative effects in accordance with the different protein types. For this purpose, four experimental groups were set up. As for the protein source casein, isolated soy protein was supplemented to the rats, together with hot water soluble extract from green tea. Four experimental groups kept eight Sprague-Dawley rats respectively. The CP group was supplemented with casein only, the CG group was supplemented with casein and hot water soluble extract from green tea, the ISP group was supplemented with isolated soy protein only, and the ISG group was supplemented with the isolated soy protein with hot water soluble extract from green tea. After 4 weeks of feeding with experimental diet, the levels of serum and liver lipid and antioxidant enzyme activity and TBARS in the liver were measured. The results are; 1. Weight gain and FER were higher in the casein group than in the isolated soy protein group in general. In the casein group, the weight gain and FER were reduced significantly when hot water soluble extract from green tea was supplemented (P < 0.05). There was no significant difference in feed intake. 2. In general, total cholesterol and LDL-cholesterol in the serum were higher in the casein group than in the isolated soy protein group, however just the concentration of LDL-cholesterol in the casein group was significantly lower when the hot water soluble extract from green tea was supplemented (P < 0.05). 3. Triglycerides in the liver were higher in the casein group than in the isolated soy protein group general, however when hot water soluble extract from green teas was supplemented only in the isolated soy protein group, the content of triglyceride in liver was significantly lower (P < 0.05). 4. There was no significant difference in antioxidant enzyme activity in the liver in all the groups, however the content of TBARS was low only in the casein group when hot water soluble extract from green tea was supplemented (P < 0.05).

• Applied Biological Chemistry
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• v.23 no.1
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• pp.14-22
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• 1980

White and black sesame produced in Korea were defatted with ethyl ether or n-hexane. Defatted sesame meal was extracted with water and salt solution, and protein extraction was precipitated at various pH 1 through 12, with trichloro acetic acid (TCA), tannic acid and ammonium sulfate, respectively. Protein was purified by Sephadex A-25, G-75, G-100 and G-200, and identified its protein fraction by polyacrylamide gel electrophoresis. Amino acids composition of protein in white sesame was analyzed by automatic amino acid analyzer. Protein contents of white sesame, black sesame and sesame meal are 20.5%, 19.2%, and 44.7%, respectively. n-Hexane was the most suitable solvent for extraction of oil from sesame. Crude protein precipitation was better in higher pH. The protein extraction was more effective with the solution containing sodium chloride tinder the pH 8. Globulin in total protein was high and prolamin was less than in other cereal proteins. Glutamic acid contents of white sesame and sesame globulin were 17.1%, and 20%, respectively. Both proteins contained relatively high levels of essential amino acids. 12-13 bands were found in water soluble protein and 2 bands in salt soluble protein were detected by the disc gel electrophoresis, and were identified in both of white and black sesame. The salt soluble protein of white sesame could be purified by Sephadee G-100 and G-200.

• Asian-Australasian Journal of Animal Sciences
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• v.21 no.3
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• pp.364-370
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• 2008

Chemical analysis and in vitro studies were conducted to investigate the nutritive value for ruminants of cell mass from lysine production (CMLP) which is a by-product of the lysine manufacturing process. Proximate analysis, protein fractionation, and in vitro protein degradation using protease from Streptomyces griseus and strained ruminal fluid were carried out to estimate ruminal protein degradability of CMLP with two reference feedstuffs-soybean meal (SBM) and fish meal (FM). Amino acid composition and pepsin-HCl degradability were also determined to evaluate postruminal availability. CMLP contained 67.8% crude protein with a major portion being soluble form (45.4% CP) which was composed of mainly ammonium nitrogen (81.8% soluble CP). The amount of nucleic acids was low (1.15% DM). The total amount of amino acids contained in CMLP was 40.60% DM, which was lower than SBM (47.69% DM) or FM (54.08% DM). CMLP was composed of mainly fraction A and fraction B2, while the protein fraction in SBM was mostly B2 and FM contained high proportions of B2 and B3 fractions. The proportion of B3 fraction, slowly degradable protein, in CP was the highest in fish meal (23.34%), followed by CMLP (7.68%) and SBM (1.46%). CMLP was degraded up to 51.40% at 18 h of incubation with Streptomyces protease, which was low compared to FM (55.23%) and SBM (83.01%). This may be due to the insoluble portion of CMLP protein being hardly degradable by the protease. The in vitro fermentation by strained ruminal fluid showed that the amount of soluble fraction was larger in CMLP (40.6%) than in SBM (17.8%). However, because the degradation rate constant of the potentially degradable fraction of CMLP (2.0%/h) was lower than that of SBM (5.8%/h), the effective ruminal protein degradability of CMLP (46.95%) was slightly lower than SBM (53.77%). Unavailable fraction in the rumen was higher in CMLP (34.0%) compared to SBM (8.8%). In vitro CP degradability of CMLP by pepsin was 80.37%, which was lower than SBM (94.42%) and FM (89.04%). The evaluation of protein degradability using different approaches indicated that soluble protein in CMLP may supply a large amount of ammonia in the rumen while insoluble protein can be by-passed from microbial attacks due to its low degradability. The results from this study suggest that CMLP can be used as a protein supplement to ruminants for supplying both non-protein nitrogen to rumen microbes and rumen undegradable protein to the host animal.

• Applied Biological Chemistry
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• v.34 no.1
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• pp.38-42
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• 1991

Salt-soluble protein contents of green and mature persimmon were 1.5 and 2.0mg/100g-fr. wt., respectively, but that of soft persimmon was 58.9mg/100g-fr. wt.. Protein contents of cell wall increased during maturation but decreased in soft persimmon. The chromatograms of salt-soluble proteins by gel filtration were similar during maturation but those of protein extracted from soft persimmon were different from those of persimmon during maturation. The cell wall protein of persimmon was of two kinds and released during softening.

• Proceedings of the Korean Society for Food Science of Animal Resources Conference
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• 2004.05a
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• pp.198-201
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• 2004

To investigate hydrostatic pressure (HP) effect on myofibrillar protein (Mf) extracted from bovine Semitendinosus muscle, Ca- and Mg-ATPase activities to evaluate denaturation of myosin and actin, and soluble protein contents were observed. In Mf treated with 100 MPa for 5 min was not observed denaturation of myosin and actin. In Mf treated with 200 MPa for 5 min, denaturation of myosin and actin were observed but inactivation rate was low (0.0136 $min^{-1}$). Inactivation rate of myosin and actin was dramatically increased above 300 MPa treatment. However denaturation of myosin and actin was not that critical with duration time. By increasing pressure size, the amount of myosin and actin in soluble protein eluted in 20 mM potassium phosphate buffer (pH 7.0) containing 0.6 M NaCl were decreased. SDS-PAGE of soluble protein released from Mf suspension in 0.1 M NaCl buffer (pH 7.0) showed that low molecular weight proteins (15${\sim}$36 KDa) were released by HP treatment above 200 MPa. From the results, denaturation of myosin and actin, and release of light molecule proteins of Mf were observed by HP treatment over 200 MPa.

• Journal of Microbiology and Biotechnology
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• v.6 no.6
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• pp.474-481
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• 1996

Since the commercially available rabbit anti-cyclin D3, generated from c-terminal 16 amino acid residues which are common to human and murine cyclin D3, is highly cross-reactive with many other cellular proteins of mouse, a new rabbit polyclonal anti-cyclin D3 has been raised by using murine cyclin D3 protein expressed at a high level in Escherichia coli as the immunogen. To express murine cyclin D3 protein in E. coli, the cyclin D3 cDNA fragment encoding c-terminal 236 amino acid residues obtained by polymerase chain reaction (PCR) was inserted into the NcoI/BamHI site of protein expression vector, pET 3d. Molecular mass of the cyclin D3 overexpressed in the presence of IPTG (Isopropyl $\beta$-D-thiogalactopyranoside) was approximately 26 kDa as calculated from the reading frame on the DNA sequence, and the protein was insoluble and mainly localized in the inclusion bodies that could be easily purified from the other cellular soluble proteins. When renaturation was performed following denaturation of the insoluble cyclin D3 protein in the inclusion bodies using guanidine hydrochloride, 4.4 mg of soluble form of cyclin D3 protein was produced from the transformant cultured in 100ml of LB media under the optimum conditions. Four-hundred micrograms of the soluble form of cyclin D3 protein was used for each immunization of a rabbit. When the antiserum obtained 2 weeks after tertiary immunization was applied to Western blot analysis, it was able to detect 33 kDa cyclin D3 protein in both murine lymphoma cell line BW5147.G.1.4 and human Jurkat T cells at 3,000-fold dilution with higher specificity to murine cyclin D3, demonstrating that the new rabbit polyclonal anti-murine cyclin D3 generated against c-terminal 236 amino acid residues more specifically recognizes murine cyclin D3 protein than does the commercially available rabbit polyclonal antibody raised against c-terminal 16 amino acids residues.

• Journal of Plant Biology
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• v.16 no.1_2
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• pp.30-38
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• 1973

To study the response to plant growth by the environmental factors, the effects of application of nitrogen on changes in the yield, crude protein, amino acids, chlorophyll, carotene, total phosphorus, acid-soluble phosphorus, phospholipids, RNA, and DNA were investigated with westerworlds 9Lolium sublatum) and perennial rye-grasses (Lolium perenne). The amounts of dry weight, crude protein, amino acids, chlorophyll, carotene, total phosphorus, acid-soluble phosphorus, phospholipids, RNA and DNA of both rye-grasses increased with adequately increasing nitrogen, and reached a maximum with an adequate application of nitrogen. The relationships between yields and crude protein contents, crude protein and RNA contents, and yields and RNA contents of westerworlds and perennial rye-grasses were found to be positively correlated, respectively. Therefore, in general, the response to plant growth by the environmental factors such as nitrogen nutrient may be summarized as follows: Environmental factors\longrightarrowDNA\longrightarrowRNA\longrightarrowProtein\longrightarrowPlant growth

• Toxicological Research
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• v.14 no.3
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• pp.371-377
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• 1998

We have cloned a soluble type human folate receptor(hFR type${\gamma}$) from human thymus cDNA library using the PCR amplification technique. To examine whether hFR type${\gamma}$ has a folate transport activity, CHO cells were transfected with the pcDNAhFR${\gamma}$ expression plasmid, and the stable cell line CHO/hFR${\gamma}$ expressing a high level of the hFR type${\gamma}$ was identified by northern and western blot analysis. The CHO/hFR${\gamma}$ cells produced a [$H^3$]folic acid binding protein in the culture medium. However, we couldn't detect any cell surface [$H^3$] folic acid binding and transport activities. The growth of the CHO/hFR${\gamma}$ cells was more rapidly inhibited than the wild type CHO cells in the low concentration folic acid media. These observations indicate that although soluble type human folate receptor can bind [$H^3$]folate, it does not involve in folate transport.

• Journal of Microbiology and Biotechnology
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• v.12 no.6
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• pp.1002-1005
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• 2002

The effects of GroEL/ES chaperone on the production of soluble form of B. macerans cyclodextrin glucanotransferase (CGTase) in recombinant E. coli were investigated. The cgt gene and groEL/ES genes are under the control of T7 promoter and Pzt-1 promoter, respectively. The optimal concentrations of inducers, IPTG and tetracycline, were found to be 1.0 mM and 10 ng/ml, respectively. When tetracycline and IPTG were added at the early exponential phase (2h) and exponential phase (3h) of growth, respectively, about 1.5-fold increase of soluble CGTase activity and 1.6-fold increase of soluble CGTase protein were obtained. An SDS-PAGE analysis revealed that about $37.2\%$ of total CGTase protein was in the soluble fraction when GroEL/ES chaperone was overexpressed.

• Asian Journal of Turfgrass Science
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• v.9 no.4
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• pp.331-342
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• 1995

An investigation was performed to reveal the removal rates of organic constituents of the litters in a Phragmithea longivalvis grassland in a Delta of the Nakdong River, The removal rates of the inorganic and organic materials are determined by the mathematical models. The removal rates and time required to decay up to a percentage of each organic constituent were calculated using these new models. The removal rates of cold water soluble fractions, other carbohydrates, hot water soluble fractions, cellulose, crude fat, lignin and crude protein were 2.67, 1.39, 1.25, 1.02, 0.92, 0.49 and 0.47, respectively, The periods required to reach half time to the steady state of the removal and accumulation for cold water soluble fractions, other carbohydrates, hot water soluble fractions, cellulose, crude fat, lignin and crude protein of the litter were 0.26, 0.50, 0.55, 0.68, 0.75, 1.41 and 1.48 years, respectively.