A series of feeding experiments were conducted to study the possible utilization of blood meal as a dietary protein source in growing common carp, Cyprinus carpio. Diets were formulated on isonitrogenous and isocaloric basis of $40\%$ crude protein and 3,640 kcal/kg diet : diet 1 (100 FMP, control), $100\%$ fish meal Protein (FMP) : diet 2 (25 BMP), $75\%$$FMP+25\%$ blood meal protein (BMP) : diet 3 (50 BMP), $50\%$$FMP+50\%$ BMP : diet 4 (75 BMP), $25\%$$FMP+75\%$ BMP : d;et 5 (100 BMP), $100\%$ BMP. As the dietary protein sources, $34.2\%$ of animal protein were supplied by FMP and/or BMP, and approximately $65.8\%$ of plant protein were used. In the first experiment, weight gain and feed efficiency were improved with increased level of blood meal protein in the diets. Weight gain and feed efficiency from fish fed diets 4 and S were significantly higher (P<0.05) than those from fish fed diets 1, 2 and 3. The second experiment was designed as a cross-over study to prove the first experiment's results. This cross-over study shows that weight gain from fish fed diet 5 is greater than that from fish fed diet 1. The third experiment was conducted to compare palatability between diet 1 (100 FMP) and 5 (100 BMP). The data from this palatability study indicated that the palatability of diet 5 was lower than that of diet 1 initially, however, the palatability of iiet 5 was improved and not worse than that of diet 1 within a week. Therefore, these findings may suggest that the fish meal can be replaced with blood meal completely in growing common carp diets.
To investigate the effects of crude protein and thyroxine on growth performance, nutrient utilizability, carcass composition, the content of total fat and cholesterol in leg muscle, breast muscle and liver, and caloric efficiency in broiler chicks. The experiment involved 3 levels of dietary crude protein (1-3 weeks: 20, 23, 26%; 4-6 weeks: 17, 20, 23%) and 3 levels of thyroxine (0.0, 1.5, 3.0 mg/kg). In the starting period (1-3 weeks), body weight gain of chicks fed diets containing 26% crude protein and 1.5 mg/kg thyroxine was higher than any other groups, and among thyroxine levels, 3.0 mg/kg thyroxine groups were lower. The best feed efficiency was obtained at 26% crude protein with no thyroxine supplemented or 1.5 mg/kg thyroxine supplemented groups. In the finishing period (4-6 weeks) the highest body weight gain was obtained at 23% crude protein with no thyroxine supplemented group. Feed intake of 17% crude protein with 1.5 mg/kg thyroxine supplemented group was higher than those of the other groups. It was found that the utilizability of crude protein in the starting period, showed the best utilizability at 20% crude protein with 1.5 mg/kg thyroxine group. Increasing crude protein level from 17 to 23%, utilizability of crude fat was decreased. The carcass composition was significantly (p<0.05) influenced by crude protein and thyroxine. Increasing thyroxine level from 0.0 to 3.0 mg/kg, crude protein content was increased whereas, crude fat content was decreased. Chicks fed diet containing 1.5 mg/kg thyroxine showed the lowest total fat content in liver tissue. In breast muscle, it was significantly (p<0.05) affected by crude protein and thyroxine. Present data revealed that the cholesterol content was increased for the chicks fed 3.0 mg/kg thyroxine. It the caloric efficiency, chicks fed a diet containing 20% crude protein with no thyroxine supplementation showed the highest caloric efficiency and the lowest efficiency was from 23% crude protein group with 1.5 mg/kg thyroxine. From this study it may be concluded that crude fat content of carcass could be successfully reduced by dietary supplementation of thyroxine, whereas crude protein content was increased.
In the present study, different expression of protein from Taekwang was revealed by 2-DE, and expressions of protein on each week after flowering was investigated. After analysis of expression of protein, MALDI-TOF was executed to identify expected protein function. Results revealed that there were three patterns of expression of protein during the maturing. The first pattern was that proteins were gradually expressed as up-regulation from 1 week to 6 week. The second pattern was that proteins were expressed gradually from 1 week to 5 week and then it started down-regulation in 6 week. The last pattern was that proteins were gradually as up-regulation from 1 week to 3 week and then down-regulation until 6 week. This phenomenon suggests that young stage has more protein related to correspondence mechanism against disease and growth and then maturing stage has more expression of protein related to storage protein. In MALDI-TOF analysis, p24 oleosin isoform A protein was identified that relates oleosin which is synthetic product in oil body. This protein spot increased gradually until 5 week and then decreased after 5 week. It explained that the protein is active until maturing stage to protect oil in seed and then its activity has gradually degraded. This result may be expected that a protein, related to growth of a seed has increased until maturing and then a seed fills up with a storage protein.
Kim, Jae-Yeol;Park, Jae-Suk;Lee, Gwi-Lae;Yoo, Chul-Gyu;Kim, Young-Whan;Han, Sung-Koo;Shim, Young-Soo
Tuberculosis and Respiratory Diseases
/
v.44
no.2
/
pp.338-348
/
1997
Background : Endotoxin, the component of outermembrane of gram negative organism, plays an important role in the initiation and amplification of inflammatory reaction by its effects on inflammatory cells. Until recently, there have been continuing efforts to delinate the mechanisms of the signal trasduction pathway of endotoxin stimuli on inflammatory cells. By uncovering the mechanisms of signal transduction pathway of endotoxin stimuli, we can expect to have tools to control the excessive inflammatory responses which sometimes may be fatal to the involved host. It was generally accepted that endotoxin exerts its inflammatory effects through inflammatory cytokines that are produced by endotoxin-stimulated inflammatory cells and there were some reports on the importance of protein kinase C and protein tyrosine kinase activation in the production of inflammatory cytokines by endotoxin So we evaluated the effect of pretreatment of protein kinase C inhibitors (H7, Staurosporin) and protein tyrosine kinase inhibitors(Herbimycin, Genistein) on the endotoxin-stimulated cytokines(IL-8 & TNF-$\alpha$) mRNA expression. Method : Peripheral blood monocytes were isolated from healthy volunteers by Ficoll-Hypaque density gradient method and purified by adhesion to 60mm Petri dishes. Endotoxin(LPS 100ng/ml) was added to each dishes except one control dish, and each endotoxin-stimulated dishes was preincubated with H7, Staurosporin(protein kinase C inhibitor), Herbimycin or Genistein(protein tyrosine kinase inhibitor) respectively except one dish. Four hours later the endotoxin stimulation, total RNA was extracted and Northern blot analysis for IL-8 mRNA and TNF-$\alpha$ mRNA was done. Result : Endotoxin stimulation increased the expression of IL-8 mRNA and TNF-$\alpha$ mRNA expression in human peripheral blood monocyte as expected and the stimulatory effect of endotoxin on TNF-$\alpha$ mRNA expression was inhibited by protein kinase C inhibitors(H7, Staurosporin) and protein tyrosine kinase inhibitors (Herbimycin, Genistein). The inhibitory effect of each drugs was increased with increasing concentration. The stimulatory effect of endotoxin on IL-8 mRNA was also inhibited by H7 and protein tyrosine kinase inhibitors (Herbimycin, Genistein) dose-dependently but not by Staurosporin. Conclusion : Protein kinase C and protein tyrosine kinase are involved in the endotoxin induced signal transduction pathway in human peripheral blood monocyte.
There are many different surface technologies currently applied for preparation of protein chips. However, it requires innovative surface chemistry for capture proteins to be immobilized on chip surface keeping their conformation and activity intact and their orientation right, while they bind tightly and densely in a given array spot. Proteogen has developed 'ProteoChip BP' coated with novel proprietary linker molecules $(ProLinker^{TM})$ for efficient and robust immobilizations of capture proteins by improving surface properties of molecular captures. It was demonstrated that $ProLinker^{TM}$ gave the best surface performance in preparation of protein microarray chip base plates among others currently available on the market. In particular, the $ProLinker^{TM}-based$ surface chemistry has demonstrated to provide excellent performance in preparation of 'Antibody Chip' for analysis of biomarkers as well as proteome expression profiles. The linker molecule has also shown to be well applicable for development of biosensors and micro-beads as well as protein microarray and nano-array. ProteoChip BP can be used either for preparation of high-density array by using a microarrayer or for preparation of 'Well-on-a-Chip' with low density array, which is better applicable for quantitative analysis of biomarkers or protein-protein interactions. The biomarker assay can be performed either by direct or sandwich methods of fluorescence immunoassay. Application of ProteoChip BP has been well demonstrated by the extensive studies of 1) tumor-marker assays, 2) new drug screening by using 'Integrin Chip' and 3) protein expression profile analysis. Some of experimental results will be presented.
Immunohistochemical studies on S-100 protein and lactoferrin were carried out to evaluate the existence and distribution pattern of S-100 protein and lactoferrin positive cells in salivary gland tumors. The specimens used were 25 cases of pleomorphic adenoma, 2 cases of monomorphic adenoma, 2 cases of mucoepidermoid tumor, 2 cases of acinic cell tumor, 3 cases of adenoid cystic carcinoma and 2 cases of adenocarcinoma occured in parotid and submandibular salivary gland. ABC kits(Dako corp. Copenhagen. Denmark) for S-100 protein and lactoferrin were used. The results obtained were summarized as follows: In the normal salivary gland. positive immunoreaction for S-100 protein was observed in myoepithelial cells of acini and intercalated ducts. Positive immunoreaction for lactoferrin was observed in serous acinic cells, epithelial cells of intercalated ducts, and excretory material in the ductal lumina. In the pleomorphic and monomorphic adenomas. most of tumor cells were positive for S-100 protein, while luminal tumor cells in gland-like or duct-like structures were rarely positive for lactoferrin. In mucoepidermoid tumor, most of squamous cells and a few of intermediate cells were positive for S-100 protein, but all of tumor cells were negative for lactoferrin. In acinic cell tumor, most of tumor cells were positive for lactoferrin, but all of tumor cells were negative for S-100 protein. In adenoid cystic carcinoma, basaloid tumor cells in trabecular structure were focally positive for S-100 protein. and in adenocarcinoma, many of tumor cells were posivive for both S-100 protein and lactoferrin. Thus, according to the embryonic stage of the development of the tumor cell origin, it was possible to classify the salivary gland tumor as followings: mucoepidermoid carcinoma which originated from the earliest stage, acinic cell tumor which originated from the end stage. Between these two extremes, there were pleomorphic adenoma, adenoid cystic carcinoma and adenocarcinoma which originated in the middle stage of the development of .the salivary glands. Based on the above results, it can be stated that S-100 protein is demonstrated in tumor cells orginated from myoepithelial cells and lactoferrin in glandular differentiated tumor cells.
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.
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.
Protein interaction network contains a small number of highly connected protein, denoted hub and many destitutely connected proteins. Recently, several studies described that a hub protein is more likely to be essential than a non-hub protein. This phenomenon called as a centrality-lethality rule. This nile is widely credited to exhibit the importance of hub proteins in the complex network and the significance of network architecture as well. To confirm whether the rule is accurate, we Investigated all protein interaction DBs of yeast in the public sites such as Uetz, Ito, MIPS, DIP, SGB, and BioGRID. Interestingly, the protein network shows that the rule is correct in lower scale DBs (e.g., Uetz, Ito, and DIP) but is not correct in higher scale DBs (e.g., SGD and BioGRID). We are now analyzing the features of networks obtained from the SGD and BioGRD and comparing those of network from the DIP.
Biodegradable polymeric microspheres were studied for their usefulness as carriers for the delivery of vaccine antigens. However, protein antigen could be denatured during microencapsulation processes due to the exposure to the organic phase and stress condition of cavitation and shear force. Therefore this study was carried out to re-evaluate the degree of protein denaturation during microencapsulation with poly(lactide-co-glycolide) (PLGA) copolymer. PLGA microspheres containing ovalbumin (OVA), prepared by W/O/W multiple emulsification method, were suspended in pH 7.4 PBS and incubated with shaking at $37.5^{\circ}C$. Drug released medium was collected periodically and analyzed for protein contents by micro-BCA protein assay. In order to evaluate the protein integrity, release medium was subjected to the analyses of SDS-PAGE and size exclusion chromatography (SEC). And enzyme-linked immunosorbent assay (ELISA) was introduced to measure the immunoreactivity of entrapped OVA and to get an insight into the three-dimensional structure of epitope. The structures of entrapped protein were not affected significantly by the results of SDS-PAGE and SEC. However, immunoreactivity of released antigen was varied, revealing the possibility of protein denaturation in some microspheres when it was evaluate by ELISA method. Therefore, in order to express the degree of protein denaturation, antigenicity ratio (AR) was obtained as follows: amount of immunoreactivity of OVA/total amount of OVA released ${\times}100(%)$. ELISA method was an efficient tool to detect a protein denaturation during microencapsulation and the comparison of AR values resulted in more accurate evaluation for immunoreactivity of entrapped protein.
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