• Title/Summary/Keyword: Protein A

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Effect of water temperature on protein requirement of Heteropneustes fossilis (Bloch) fry as determined by nutrient deposition, hemato-biochemical parameters and stress resistance response

  • Fatma, Shabihul;Ahmed, Imtiaz
    • Fisheries and Aquatic Sciences
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    • v.23 no.1
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    • pp.1.1-1.14
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    • 2020
  • Background: Dietary protein requirements are dependent on a variety of factors and water temperature is one of the most important abiotic factors affecting protein requirement of fish. This study was, therefore, conducted to investigate effects of water temperature on dietary protein requirement of fry Heteropneustes fossilis which has high demand in most of the Asian markets. Methods: Quadruplicate groups of 30 fish per treatment (2.97 ± 0.65 cm; 5.11 ± 0.34 g) were fed seven isoenergetic diets (17.9 kJ g-1 gross energy; 14.99 kJ g-1 digestible energy) containing dietary protein levels ranging from 28 to 52% at two water temperatures (18 and 26 ℃). Experimental diets were fed to apparent satiation as semi-moist cakes thrice daily at 17:00, 12:00, and 17:30 h for 12 weeks. For precise information, various growth parameters, protein deposition, hematological parameters, metabolic enzymes, and stress response were analyzed, and effects of water temperature on dietary protein requirement was recommended on the basis of response from above parameters. Results: Groups held at 26 ℃ attained best growth, feed conversion, and protein deposition at 44% dietary protein indicating that temperature affected dietary protein requirement for optimum growth of H. fossilis fry and protein requirement seems to be satisfied with 44% dietary protein. Interestingly, interactive effects of both dietary protein levels and temperature were not found (P > 0.05). Fish reared at 18 ℃ had comparatively higher values for aspartate and alanine transferases than those reared at 26 ℃ water temperature which exhibited normal physiological value for these enzymes indicating that body metabolism was normal at this temperature. Hematological parameters also followed same pattern. Furthermore, fish reared at 26 ℃ water temperature exhibited more resistant to thermal stress (P < 0.05). The 95% maximum plateau of protein deposition data using second-degree polynomial regression analyses exhibited dietary protein requirement of fry H. fossilis between 40.8 and 41.8% of diet at 26 ℃ water temperature. The recommended range of dietary protein level and protein/digestible energy ratio for fry H. fossilis is 40.8-41.8% and 27.21-27.88 mg protein kJ-1 digestible energy, respectively. Conclusions: Information developed is of high significance for optimizing growth potential by making better utilization of nutrient at 26 ℃ and, to develop effective management strategies for mass culture of this highly preferred fish species.

Identification of the Protein Function and Comparison of the Protein Expression Patterns of Wheat Addition Lines with Wild Rye Chromosomes (야생 호밀 염색체 첨가 밀 계통의 단백질 발현 양상 비교 분석)

  • Lee, Dae Han;Cho, Kun;Woo, Sun Hee;Cho, Seong-Woo
    • KOREAN JOURNAL OF CROP SCIENCE
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    • v.64 no.4
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    • pp.373-383
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    • 2019
  • The objectives of this study were to compare the protein expression patterns and degrees and identify the protein function of disomic addition lines (DAs) in Leymus racemosus, in order to improve the quality of wheat. Upon SDS-PAGE, L. racemosus showed two major protein bands whereas Chinese Spring (CS) had four major protein bands of high molecular weight. The DA(s) generally showed a similar protein expression pattern to that of CS, because 42 chromosomes were from CS and two chromosomes were from L. racemosus. However, only the L.r[J] line showed two protein bands of between 15 and 20 kDa, like L. racemosus. Image analysis based on 2-DE revealed that L.r[F] had the most upregulated protein spots, whereas L.r[N] had the least upregulated protein spots. For L.r[I], the frequency of the downregulated protein spots was higher than that of the upregulated ones. Using MALDI-TOF MS, the protein function was identified for each protein spot on the 2-DE polyacrylamide gel. The protein spots were classified into 11 groups according to protein function. Among the 11 groups, most protein spots of the DA(s) were identified as proteins related to metabolism. Additionally, unique protein spots of the DA(s) were related to abiotic stressors such as cold and heat. Those proteins are useful for improving wheat quality with resistance against abiotic stressors.

Role of C-terminal 7 Amino Acids of N4SSB Protein in Its in vivo Activity (N4SSB 단백질의 C-말단기의 7개의 아미노산이 N4SSB 단백질의 in vivo 활성에 미치는 영향)

  • Choi, Mieyoung
    • Korean Journal of Microbiology
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    • v.34 no.4
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    • pp.248-253
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    • 1998
  • Bacteriophage N4, a lytic phage specific for Esherichia coli K12 strain encodes single-stranded DNA-binding protein, N4SSB (bacteriophage N4-coded single-stranded DNA-binding protein). N4SSB protein is originally identified as a protein required for N4 DNA replication. N4SSB protein is also required for N4 late transcription, which is catalyzed by E. coli ${\sigma}^{70}$ RNA polymerase. N4 late transcription does not occur until N4SSB protein is synthesized. Recently it is reported that N4SSB protein is essential for N4 DNA recombination. Therefore N 4SSB protein is a multifunctional protein required for N4 DNA replication, late transcription, and N4 DNA recombination. In this study, a variety of mutant N4SSB proteins containing internal deletions or substitutions were constructed to define and characterize domains important for N4 DNA replication, late transcription, and N4 DNA recombination. Test for the ill vivo activity of these mutant N4SSBs for N4 DNA replication, late transcription, and N4 DNA recombination was examined. The results suggest that C-terminal 7 amino acid residues are important for the activity of N4SSB. Three lysine residues, which are contained in this region play important roles on N4SSB activity.

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Effect of low protein diets added with protease on growth performance, nutrient digestibility of weaned piglets and growing-finishing pigs

  • Kim, Yong Ju;Lee, Ji Hwan;Kim, Tae Heon;Song, Min Ho;Yun, Won;Oh, Han Jin;Lee, Jun Soeng;Kim, Hyeun Bum;Cho, Jin Ho
    • Journal of Animal Science and Technology
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    • v.63 no.3
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    • pp.491-500
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    • 2021
  • The objective of this study was to evaluate the effects of low protein diets added with protease on growth performance, nutrient digestibility, and blood profiles of weaned piglets and growing-finishing pigs. A total of 96 weaned pigs ([Yorkshire × Landrace] × Duroc) with average body weight (BW) of 6.99 ± 0.21 kg were used in a 20-week experiment. The dietary treatments were arranged in a 2 × 3 factorial design. Treatments were as follows: In phase 1 (1-2 weeks), two protein levels as high protein (HP; 19.0%), low protein (LP; 17.0%), and three protease (PT) levels (PT0, 0%; PT1, 0.3%; and PT2, 0.5%); in phase 2 (3-4 weeks), protein levels (HP, 18.05%; LP, 16.15%) and protease levels (0%, 0.3%, and 0.5%); in phase 3 (5-12 weeks), protein levels (HP, 17.1%; LP, 15.3%) and protease level (0%, 0.15%, and 0.3%); in phase 4 (13-20 weeks), protein levels (HP, 16.15%; LP, 14.45%) and protease level (0%, 0.15%, and 0.3%). At 4 weeks and 20 weeks after treatment, BW was higher (p < 0.050) in the PT2 group than PT0 group. From weeks 0 to 4, average daily gain (ADG) and feed efficiency (G/F) were higher (p = 0.006 and p = 0.014; p = 0.014 and p = 0.044, respectively) in the PT2 group than PT0 and PT1 groups. From weeks 16 to 20, ADG and G/F were higher (p < 0.001 and p = 0.009; p = 0.004 and p = 0.033, respectively) in the PT2 group than PT0 and PT1 groups. Crude protein (CP) digestibility was higher (p = 0.013, p = 0.014, and p = 0.035, respectively) in the low protein (LP) group than high protein (HP) group at weeks 4, 12, and 20. At weeks 4 and 20, the LP diet group had lower (p < 0.001 and p = 0.001, respectively) blood urea nitrogen (BUN) levels than the HP diet group. Therefore, a low CP diet added with protease could increase growth performance and CP digestibility of weaned piglets and growing-finishing pigs.

Immunohistochemical Studies on S-100 Protein and Lactoferrin in Salivary Gland Tumors (타액선 종양에 있어서 S-100 단백과 Lactoferrin에 관한 면역조직화학적 연구)

  • Choi Dae-Sik;Kim Sang-Hyo
    • Korean Journal of Head & Neck Oncology
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    • v.9 no.1
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    • pp.74-87
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    • 1993
  • 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.

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Separation and Composition of Sesame Meal Protein (참깨박(粕) 단백질(蛋白質)의 분리(分離)와 조성(組成))

  • Kim, Jun-Pyong;Shim, Woo-Man;Kim, Chong-Ik
    • 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.

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Antigenicity of Protein Entrapped in Poly(lactide-co-glycolide) Microspheres (폴리락티드-글리콜리드 마이크로스피어에 봉입된 단백질의 항원성 평가)

  • Song, Seh-Hyon;Cho, Seong-Wan;Shin, Taek-Hwan;Yoon, Mi-Kyoung;Choi, Young-Wook
    • Journal of Pharmaceutical Investigation
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    • v.31 no.3
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    • pp.191-196
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    • 2001
  • 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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A Study on the Long-Term Effects of Dietary Protein Level on Ca and Skeletal metabolism in Ovariectomized Rats (장기간의 고.저단백식이섭취가 난소절제쥐의 Ca 및 골격대사에 미치는 영향)

  • 김화영
    • Journal of Nutrition and Health
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    • v.28 no.5
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    • pp.415-425
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    • 1995
  • This study was performed to investigate the effect of dietary protein level on the metabolic changes of Ca and skeletons in postmenopausal women, using ovariecotomized rats as an animal model. The female rats of 200∼250g were fed either 8%(L) or 50%(H) casein diet for 15 weeks(1st experiment). At 15th week, the rats of each diet group were undergone ovariectomy or sham-operation and they were continued to feed the same experimantal diet for 9 more months(2nd experiment). Ca metabolism, kidney function and bone composition were determined at the end of 1st experiment, 3rd and 9th month of 2nd experiment. After 1st experiment, high protein group showed higher urinary Ca and protein excretion, however, there was no difference in GFR and urinary hydroxyproline excretion. The weights, ash and Ca content of femur, scapular and vertebra tended to be higher in high protein groups which tells that high protein promoted skeletal growth. In 2nd experiment, high protein group showed higher urinary Ca and protein excretion and lower Ca absorption and balance. GFR was not affected by dietary protein and ovariectomy but increased with time, as well as kidney weight which shows the continuous development of kidney at this age of 15 month in rats. There were no difference in urinary hydroxyproline, serum ALP, and PTH among experimental groups. The weights of femur, scapular, 4th vertebra increased with time, showing the skeleton continues to grow at this age in rats. However, Ca contents, Ca/wt, Ca/ash were decreased with time and tended to be lower in high protein group especially in femur. In conclusion, prolonged feeding of high protein diet deteriorated Ca metabolism and induced bone loss as time after menopause is extended.

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Effect of Dietary Protein and Fat Levels on the Utilization of Nitrogen and Energy and Body Composition in Rats (식이중 단백질과 지방수준이 흰쥐의 성장, 질소와 에너지 이용 및 체조성에 미치는 영향)

  • 권순형
    • Journal of Nutrition and Health
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    • v.20 no.2
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    • pp.122-134
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    • 1987
  • In order to investigate the effect of dietary protein and fat levels on the growth and the utilization of nitrogen and energy and body composition in rats, Sprague\ulcornerDawley 48 male rats of 8 weeks old weighing approxijIlately 215-220g were subjected to feeding trials for 8 weeks and then subsequently to metabolic trials for 2 weeks. Four dietary protein levels (4, 8, 16, 32%) and each protein level contained two fat levels(3.9, 11.7%=1O,3J% of 3600kcal ME/kg) by addition of an appropriate amount of carbo\ulcornerhydrate and the following results were obtained. The body weight gain and food efficiency ratio of the rats to which a diet of 16% protein and 3.9% fat was fed were significantly higher than in either case of 8% pro\ulcornertein diet or of 32% protein diet. The digestibility of protein in the experimental diets was 73.3 -93.4%. The digesti\ulcornerbility of energy ( energy absorption) in the experimental diets was 83.2 -91.5%. The utilization of protein and the metabolic energy efficiency in the experimental diets was highest at the diet of 8% protein and 3.9% fat. The analysis of the body composition after feeding trials for 8 weeks has shown that the content of body water and protein were not affected by protein and fat levels in diet. The content of body fat in the rats to which 3.9% fat diet was fed was high\ulcornerer than that in those to which 11.7% fat diet was fed. From the above experimental results it may be suggested that the best formula of diet for the 8 weeks old rats may be composed of the 8% protein and 3.9% fat.

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Effect of Protein Sources on Rumen Microbial Protein Synthesis Using Rumen Simulated Continuous Culture System

  • Joo, J.W.;Bae, G.S.;Min, W.K.;Choi, H.S.;Maeng, W.J.;Chung, Y.H.;Chang, M.B.
    • Asian-Australasian Journal of Animal Sciences
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    • v.18 no.3
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    • pp.326-331
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    • 2005
  • A rumen simulated continuous culture (RSCC) system was used to study the influence of supplementation of the three different types of protein sources such as urea, casein and soy protein on rumen microbial synthesis in terms of rumen microbial synchronization. The urea treatment showed the highest pH value. Ammonia nitrogen concentration was rapidly increased after feeding and not significantly different in the urea treatment (13.53 mg/100 ml). Protozoa numbers were not significantly different for soy protein and casein treatment compared to urea treatments during incubation. The average concentration of total VFA (mMol) was not detected with significant difference among treatments, but iso-butyrate production showed the highest for soy protein treatment among treatments (p<0.001). The lowest concentration in total iso-acids (iso-butyrate and iso-valerate) production was observed in urea treatment. The soy protein treatment showed no significantly change in acetate/propionate. The amounts of dry matter (DM) out flow showed no significant difference among treatments. Organic matter (OM) flow was the highest for urea treatments and the lowest for casein treatment (p<0.03). The nitrogen flow for casein treatment was not significantly different from other treatments. The efficiency of microbial protein synthesis in terms of microbial nitrogen (MN) synthesis (g MN/kg ADOM) digested in the rumen was highest for casein treatment (58.53 g MN/kg ADOM) compared to soy protein and urea (p<0.05). This result suggests that rumen ammonia releasing rate may influence on microbial protein synthesis in the rumen.