• Journal of Sericultural and Entomological Science
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• v.24 no.2
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• pp.55-72
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• 1983

These studies were done to find out any difference, ultrastructural, physical or chemical, between the shells of diapausing and non-diapausing eggs of the silkworm, Bombyx mori L. 1. From the electron-microscopic observation, the egg shells have four distinctive layers. In addition to the four layers, the shells in the diapausing eggs has another layer with low electron density on its surface. 2. The permeability of the egg shell to hydrochloride was much lower in diapausing egg than in non-diapausing egg. Also the permeability changed in the opposite directions with the egg age: the diapausing eggs decreased while non-diapausing ones increased. 3. The permeability increased when the diapausing egg shell was treated with HCl. When they were treated with ether, however, the increase in permeability was much smaller. It seems there was an ether soluble material involved in the content of the egg shell. 4. The diapausing eggs were also much more resistant to desiccation than the non-diapausing ones. The former, when treated with HCl or chilling, became less resistant to desiccation. 5. The positive histochemical response of the egg shell to PAS-Alcian blue and protein stainings suggests presence of abundant proteins and carbohydrates in the egg shell. On the other hand, the staining response to lipid was more positive in the inner layers than in the outer layer of the shell. 6. The egg shell adhesives seems to be mucopolysaccharides produced by colleterial glands, since the oviposited eggs showed a positive responses to carbohydrate and negative to lipid-staining chemicals, but not the mature oocytes in the ovarioles. 7. There were two bands on the electrophoretic pattern of the SH proteins extracted from the egg shells both in the diapausing egg and non-diapausing one: a slow moving major component and a fast moving minor one. However, the electrophoretic mobility showed a difference in the minor components between them. It is evident that the fast moving minor one of non-diapausing egg ran a little further than that of diapausing egg. 8. In amino acids analysis, no significant differences were found in their composition between diapausing and non-diapausing egg and SH proteins contain relatively more glycine and less cystine.

• Journal of Fisheries and Marine Sciences Education
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• v.3 no.2
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• pp.47-72
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• 1991

To obtain the principal data for useful treatment and processing of Korean geoduck (Panope japonica A. ADAMS) which inhabit mostly at Dong-Hae coastal area in Korea, changes of $NH_2$-N, TMAO, TMA, total creatinine, protein composition and fatty acid composition in raw and blanched geoduck muscle during storage at $-20^{\circ}C$ were investigated. In addition, its chemical composition variation in the whole year was elucidated. The moisture content in geoduck muscle meat was 78.1% to 82% in the whole year. Particularly, in July its moisture content was maximum as 82% and in September minimum as 78.1%. Crude protein was in the range of 12.3-16.4%, crude lipid the average was 1.5%, crude ash on the average was 1.4%. The abundant fatty acids in geoduck muscle oil were $C_{16}$ : 0, $C_{16}$ : 1, $C_{18}$ : 0, $C_{18}$ : 1, $C_{20}$ : 5, and $C_{22}$ : 6 acids. During storage at $-20^{\circ}C$, content of unsaturated fatty acid such as eicosapentaenoic acid (EPA, $C_{20}$ : 5) and docosahexaenoic acid (DHA, $C_{22}$ : 6)in raw geoduck muscle decreased somewhat and the raw geoduck was slightly oxidized. Trimethylamine (TMA), volatile basic nitrogen (VBN)and $NH_2$-N of raw muscle increased compared to blanched muscle. Trimethylamine oxide (TMAO) was slightly decreased during the storage period. The muscle protein was approximately composed of 37% sarcoplasmic, 29% myofibrillar, 22% alkali soluble, and 12% stroma protein. Among several proteins, myofibrillar protein content decreased mostly, while the alkali-soluble and stroma protein content increased slightly during storage at $-20^{\circ}C$.

• Parasites, Hosts and Diseases
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• v.23 no.2
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• pp.189-196
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• 1985

In order to observe the protein composltlOns of soluble extracts of P. westermani, and their changes during early developmental stages, the crude saline extracts of 4, 6, 8, 10 and 12 week-old worms which were harvested from experimentally infected dogs were analysed by disc-PAGE. The results were as follows: 1. A total of 15 bands were identified from electrophoregrams of respective developmental stages. Of them, 5 bands were recognized throughout the developmental stages. 2. The number and protein amount of identified bands changed according to the worm development from 4 weeks to 12 weeks. However, tLe bar::ding patterns of 4 and 6 week-old worms and 8 and 10 week-old worms were similar each other. 3. Of 15 identified bands, Band 1 was recognized only in 12 week-old worms whereas Bands 3, 4, 8, 9, 10, 11 and 15 gradually lowered their amount according to dcvelor:ment to disappear in 12 week-old. In addition, Band 5 became a major band in 12 week-old while Band 6 turned to a minor band at the same age. The possible relations of changing patterns of protein bands with worm development were discussed.

• Environmental Mutagens and Carcinogens
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• v.17 no.2
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• pp.97-108
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• 1997

The drugs or xenobiotics introduced to the body, are detoxified through the process of biotransformation in the body. In this process, most of the insoluble compounds become more polar, soluble and easily excretable. But, parts of introduced materials are metabolized to highly reactive electrophilic carcinogens through activation pathways. These metabolites are toxic and can react with DNA, RNA and proteins which are nucleophilic compounds. The objective of this study is to illustrate the aleactivation pathways of two highly reactive epoxide compounds, vinyl carbamate epoxide (VCO) and 2'-(4-nitrophenoxy)oxirane (NPO). They are the ultimate electrophilic carcinogens of ethyl carbamate(urethane) and 4-nitrophenyl vinyl ether, respectively. In this research, we studied the inhibition of the mutagenic activities of VCO or NPO by nuchieophiles [glutahione(GSH) and N-acetylcysteine(NAC)], detoxifying enzymes[epoxide hydrolase and glutathione-S-transferase(GST)] and intracellular organelles (microsomes and cytosol). In addition we also tested the suppression of DNA adducts formation by GSH and NAC. The results are summerized as follow. 1. The microsomes and cytosol which contain epoxide hydrolase and GST, respectively, decreased the mutagenicity of VCO (74% and 95%, respecfivel), and NPO (35% and 93%, respectively). The nucleophilic GSH and NAC decreased the mutagenicity by 86% (VCO) and 80% (NPO), 76% (VCO) and 40% (NPO), respectively. 2. The purified epoxide hydrolase decreased the mutagenicity of two epoxides in a dose-dependent manner, and GSH also decreased the mutagenicity in the presence of GST. 3. Formation of two DNA adducts, 7-(2'-oxoethyi)guanine (OEG) and N2,3-ethenoguanine(EG), were compared in the presence of calf thymus DNA and epoxide (VCO or NPO) in vitro system. The amounts of DNA adducts were decreased in the presence of GSH (25% and 29% in VCO, 32% and 29% in NPO), and NAC (14% and 16% in VCO, 21% and 11% in NPO), respectively. From these results, it is concluded that the ultimate carcinogenic metabolites, VCO and NPO, can be made in the body, but much of them may be inactivated and detoxified by the nucleophilic GSH, NAC and detoxifying enzymes (epoxide hydrolase and GST). Therefore, by these mechanism, the formation of DNA adducts and mutagenic activities of these two epoxides may be lowered in vivo.

• Journal of the Korean Society of Food Science and Nutrition
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• v.31 no.1
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• pp.1-6
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• 2002

Synthesis of new active protein was investigated by heat-treatment and fermentation of kidney beans with Bacillus subtilis ATCC 51189. The amount of water-soluble protein in raw kidney bean (raw protein, RP) was greatly reduced by heating (heated protein, HP) and several new amino acids were synthesized by fermentation. The molecular weights of proteins determined by SDS-PAGE were 118 kDa for RP and a new band of 18.0 kDa For protein (fermented protein, FP) in kidney beans heated and fermented with B. subtilis ATCC 51189. Hemagglutinating activities of RP, HP and FP were 128 HU, 4 HU and 32 HU respectively. Both of RP and FP showed anticancer activity against stomach cancer cell line (SNU-1) at 50 $\mu\textrm{g}$g/mL and lymphocyte stimulating activity at 1 $\mu\textrm{g}$/mL, and stimulated PBMC to secrete IFN-${\gamma}$ and IL-12. However, HP did not show any kinds of activities. Taken together, these results suggested that lectin in kidney beans was destroyed by heating, hut new active lectin-like Protein was derived by fermentation with B. subtilis ATCC 51189.

• Korean Journal of Food Science and Technology
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• v.24 no.3
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• pp.284-288
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• 1992

This study was undertaken to investigate the effect of pH and phytate level on the solubility of the protein due to binding between phytate and low-phytate rapeseed protein isolate by means of SDS-polyacrylamide gel electrophoresis. Results showed that the number of protein bands decreased by the increasing amount of phytate added to the soluble extract at pH 2.0 and 5.0 whereas there was no change at pH 11.5. Among 18 bands of rapeseed proteins at pH 2.0, seven bands (105.8, 52.3, 37.3, 34.8, 26.3, 21.3, 18.4 KDa) were removed by precipitation with 100 mg phytate addition and six bands (78.8, 46.5, 19.4, 16.8, 11.7, 8.5 KDa) further disappeared by 150 mg phytate addition. Among 15 bands at pH 5.0, only four bands disappeared by phytate addition. It is suggested that the functionality of rapeseed protein isolate can be improved by lowering the phytate content.

• Journal of Microbiology and Biotechnology
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• v.17 no.1
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• pp.123-129
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• 2007

The trehalose $({\alpha}-D-glucopyranosyl-[1,1]-{\alpha}-D-glucopyranose)$ biosynthesis genes MhMTS and MhMTH, encoding a maltooligosyltrehalose synthase (MhMTS) and a maltooligosyltrehalose trehalohydrolase (MhMTH), respectively, have been cloned from the hyperthermophilic archaebacterium Metallosphaera hakonesis. The ORF of MhMTS is 2,142 bp long, and encodes 713 amino acid residues constituting a 83.8 kDa protein. MhMTH is 1,677 bp long, and encodes 558 amino acid residues constituting a 63.7 kDa protein. The deduced amino acid sequences of MhMTS and MhMTH contain four regions highly conserved for MTSs and three for MTHs that are known to constitute substrate-binding sites of starch-hydrolyzing enzymes. Recombinant proteins obtained by expressing the MhMTS and MhMTH genes in E. coli catalyzed a sequential reaction converting maltooligosaccharides to produce trehalose. Optimum pH of the MhMTS/MhMTH enzyme reaction was around 5.0 and optimum temperature was around 70 C. Trehalose-producing activity of the MhMTS/ MhMTH was notably stable, retaining 80% of the activity after preincubation of the enzyme mixture at $70^{\circ}C$ for 48 h, but was gradually abolished by incubating at above $85^{\circ}C$. Addition of thermostable $4-{\alpha}-glucanotransferase$ increased the yield of trehalose production from maltopentaose by 10%. The substrate specificity of the MhMTS/MhMTH-catalyzed reaction was extended to soluble starch, the most abundant maltodextrin in nature.

• Journal of Yeungnam Medical Science
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• v.13 no.1
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• pp.46-58
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• 1996

Inositol 1,4,5-triphosphate($InsP_3$) is a second messenger for mobilizing intracellular $Ca^{2+}$. It can be dephosphorylated by soluble and particulate forms on $InsP_3$ 5-phosphatase, or phosphorylated to produce inositol 1,3,4,5-tetrakisphosphate($InsP_3$) by $InsP_3$ 3-kinase. These enzymes represent possible targets for the regulation of the $InsP_3/InsP_4$ signal. $InsP_3$ 3-kinase which catalyses th ATP-dependent phosphorylation of $InsP_3$ was purified from bovine brain tissue. All operation were carried out at $4^{\circ}C$. Fresh tissure was homogenized and centrifuged. The supernatant was pooled. Proteins were precipitated from 10% polyethylene glycol, and suspended solution was applied to DEAE cellulose column for chromatography. As the result of above procedure, two isozymes of $InsP_3$ 3-kinase, I and II were obtained. Each isozyme was applied to Matriz green gel, Calmodulin-Affigel 15 column and subsequent phenyl-TSK HPLC column. Specific activites(SA) and fold of puriety were observed at each purification step of chromatography. At DEAE cellulose chromatography, SA were I, 0.6 and II, 4.8 nM/min/mg, and folds were I, 17.2 and II, 16.6. At Matrix green gel chromatography, SA were I, 18 and II, 11 nM/min/mg, folds were I, 62.1 and II, 38.0. At calmodulin-Affigel 15 column chromatography, SA were I, 19 and II, 13 nM/min/mg, folds were I, 65.5 and II, 44.8. Finally $InsP_3$ kinase I and II were purified 3,103-fold and 2,310-fold, and SA were I, 900 and II, 670 nM/min/mg, respectively. SDS-polyacrylamide gel electrophoresis elucidated 3 distinct fractions of Mr of 145,000, 85,000 and 69,500 from isozyme I, and 2 distinct fractions of Mr of 79,000 and 57,000 from isozyme II.

• Korean Journal of Soil Science and Fertilizer
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• v.35 no.5
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• pp.314-325
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• 2002

The effects of arbuscular mycorrhizal (AM) fungus (Glomus intraradices) on plant growth and N metabolic responses were examined in perennial ryegrass plants exposed to drought-stressed or well-watered condition. Mycorrhizal inoculation improved significantly leaf water potential, dry mass and P content. Drought stress increased significantly nitrate concentration in roots where the increase was much less in AM than non-AM. Drought stress decreased the concentration of soluble proteins in non-AM shoots, whereas non-significant decline occurred in AM shoots even under drought condition. The concentrations of ammonia and proline in drought stressed non-AM plants significantly increased, while mycorrhizal inoculation lowered significantly ammonia and proline accumulation. The decrease in leaf dry weight in drought stressed-plants was significantly correlated to the increase in ammonia (p<0.01) and proline concentration (p<0.01). These results suggested that the increased P content and N assimilation by mycorrhizal inoculation may be associated with drought stress tolerance, showing the moderating effects on shoot growth inhibition and ammonia accumulation in drought stressed-plants.

• Food Science and Preservation
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• v.23 no.3
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• pp.413-421
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• 2016

The aim of this study was to investigate physicochemical properties of porcine blood hydrolyzed by proteases under various conditions for utilization as a food source. Five kinds of proteases (Alcalase, Neutrase, Protex-40L, PTPF-1430, and KMFP-15) were tested at different concentrations (0.1, 0.2, and 0.3%, w/v) during hydrolysis at 55 for 4 hr. Hydrolysis with $^{\circ}C$ KMFP-15 showed the lowest pH by 7.3. The highest soluble solid ($24.3^{\circ}Brix$) and free amino acid (4,944 mg%) contents were obtained by hydrolysis with KMFP-15 (w/v) at 0.2% addition level, which was not significantly different from the sample hydrolyzed at 0.3% level. Under the optimal condition of KMFP-15 at 0.2%, porcine blood was hydrolyzed at 60 up to 8 hr. The $^{\circ}C$ free amino acid content reached the highest at 4 hr, and then decreased with longer hydrolysis time. Under the optimal hydrolysis conditions, porcine blood hydrolysis powder had plenty of crude proteins, amino acids, and minerals, including iron, potassium, and zinc. The results showed that porcine blood could be utilized as an useful source of food supplement. The optimum conditions of hydrolyzing porcine blood, using 0.2 KMFP at $60^{\circ}C$ for 4 hr, can be used in the commercial production of protein supplements, amino acid sources, and iron fortifying agents.