• Title/Summary/Keyword: Small protein

Search Result 1,755, Processing Time 0.027 seconds

Dietary protein requirements of abalone (Haliotis discus, Reeve 1846) depending on abalone size

  • Baek, Seong Il;Cho, Sung Hwoan
    • Fisheries and Aquatic Sciences
    • /
    • v.24 no.3
    • /
    • pp.129-137
    • /
    • 2021
  • Dietary protein requirements of abalone (Haliotis discus) depending on abalone size were determined and compared. One thousand and fifty small abalone (initial weight of 2.7 g) and five hundred forty large one (initial weight of 16.0 g) were distributed into 15 and 18 containers in Trial 1 and 2, respectively. Five and six experimental diets containing crude protein level from 20% to 40% and 20% to 45% with 5% increment of protein level for the small and large abalone were prepared and referred to as the CP20, CP25, CP30, CP35, CP40, and CP45 diets, respectively. The experimental diets were fed to abalone for 16 weeks in Trials 1 and 2. Specific growth rate (SGR) of the small abalone fed the CP20 diet was lower compared to that of abalone fed all other diets in Trial 1. Growth performance (weight gain and SGR) of the large abalone fed the CP30, CP35, and CP40 diets were greater than that of abalone fed the CP20, CP25, and CP45 diets in Trial 2. Dietary protein requirements were estimated to be 33.0% and 33.5% for the small and large abalone based on the 2nd order polynomial analysis, respectively. Dietary protein requirements for the small abalone grown from 2.7 g to 7.4 g and the large one grown from 16 g to 21 g were estimated to be 33.0% and 33.5%, respectively. Size differences in abalone did not affect dietary protein requirement under this experimental conditions.

A Small Epitope Tagging on the C-Terminus of a Target Protein Requires Extra Amino Acids to Enhance the Immune Responses of the Corresponding Antibody

  • Kyungha Lee;Man-Ho Cho;Mi-Ju Kim;Seong-Hee Bhoo
    • Journal of Microbiology and Biotechnology
    • /
    • v.34 no.6
    • /
    • pp.1222-1228
    • /
    • 2024
  • Protein-specific antibodies are essential for various aspects of protein research, including detection, purification, and characterization. When specific antibodies are unavailable, protein tagging is a useful alternative. Small epitope tags, typically less than 10 amino acids, are widely used in protein research due to the simple modification through PCR and reduced impact on the target protein's function compared to larger tags. The 2B8 epitope tag (RDPLPFFPP), reported by us in a previous study, has high specificity and sensitivity to the corresponding antibody. However, when attached to the C-terminus of the target protein in immunoprecipitation experiments, we observed a decrease in detection signal with reduced immunity and low protein recovery. This phenomenon was not unique to 2B8 and was also observed with the commercially available Myc tag. Our study revealed that C-terminal tagging of small epitope tags requires the addition of more than one extra amino acid to enhance (restore) antibody immunities. Moreover, among the amino acids we tested, serine was the best for the 2B8 tag. Our findings demonstrated that the interaction between a small epitope and a corresponding paratope of an antibody requires an extra amino acid at the C-terminus of the epitope. This result is important for researchers planning studies on target proteins using small epitope tags.

Sport impact on the strength of the nanoscale protein tissues under the thermal condition

  • Xin, Fang;Mengqian, Hou
    • Advances in nano research
    • /
    • v.13 no.6
    • /
    • pp.561-574
    • /
    • 2022
  • The stability of protein tissues and protein fibers in the human muscle is investigated in the presented paper. The protein fibers are modeled via tube structures embedded in others proteins fibers like the elastic substrate. Physical sport and physical exercise play an important role in the stability of synthesis and strength of the protein tissues. In physical exercise, the temperature of the body increases, and this temperature change impacts the stability of the protein tissues, which is the aim of the current study. The mathematical simulation of the protein tissues is done based on the mechanical sciences, and the protein fibers are modeled via wire structures according to the high-order theory beams. The thermal stress due to the conditions of the sport is applied to the nanoscale protein fibers, then the stability regarding the frequency analysis is investigated. Finally, the impact of temperature change, physical exercise, and small-scale parameters on the stability of the protein tissues are examined in detail.

Analysis of protein-protein interaction network based on transcriptome profiling of ovine granulosa cells identifies candidate genes in cyclic recruitment of ovarian follicles

  • Talebi, Reza;Ahmadi, Ahmad;Afraz, Fazlollah
    • Journal of Animal Science and Technology
    • /
    • v.60 no.6
    • /
    • pp.11.1-11.7
    • /
    • 2018
  • After pubertal, cohort of small antral follicles enters to gonadotrophin-sensitive development, called recruited follicles. This study was aimed to identify candidate genes in follicular cyclic recruitment via analysis of protein-protein interaction (PPI) network. Differentially expressed genes (DEGs) in ovine granulosa cells of small antral follicles between follicular and luteal phases were accumulated among gene/protein symbols of the Ensembl annotation. Following directed graphs, PTPN6 and FYN have the highest indegree and outdegree, respectively. Since, these hubs being up-regulated in ovine granulosa cells of small antral follicles during the follicular phase, it represents an accumulation of blood immune cells in follicular phase in comparison with luteal phase. By contrast, the up-regulated hubs in the luteal phase including CDK1, INSRR and TOP2A which stimulated DNA replication and proliferation of granulosa cells, they known as candidate genes of the cyclic recruitment.

Protein Drug Oral Delivery: The Recent Progress

  • Lee, Hye-J.
    • Archives of Pharmacal Research
    • /
    • v.25 no.5
    • /
    • pp.572-584
    • /
    • 2002
  • Rapid development in molecular biology and recent advancement in recombinant technology increase identification and commercialization of potential protein drugs. Traditional forms of administrations for the peptide and protein drugs often rely on their parenteral injection, since the bioavailability of these therapeutic agents is poor when administered nonparenterally. Tremendous efforts by numerous investigators in the world have been put to improve protein formulations and as a result, a few successful formulations have been developed including sustained-release human growth hormone. For a promising protein delivery technology, efficacy and safety are the first requirement to meet. However, these systems still require periodic injection and increase the incidence of patient compliance. The development of an oral dosage form that improves the absorption of peptide and especially protein drugs is the most desirable formulation but one of the greatest challenges in the pharmaceutical field. The major barriers to developing oral formulations for peptides and proteins are metabolic enzymes and impermeable mucosal tissues in the intestine. Furthermore, chemical and conformational instability of protein drugs is not a small issue in protein pharmaceuticals. Conventional pharmaceutical approaches to address these barriers, which have been successful with traditional organic drug molecules, have not been effective for peptide and protein formulations. It is likely that effective oral formulations for peptides and proteins will remain highly compound specific. A number of innovative oral drug delivery approaches have been recently developed, including the drug entrapment within small vesicles or their passage through the intestinal paracellular pathway. This review provides a summary of the novel approaches currently in progress in the protein oral delivery followed by factors affecting protein oral absorption.

Transfer RNA-Derived Small Non-Coding RNA: Dual Regulator of Protein Synthesis

  • Kim, Hak Kyun
    • Molecules and Cells
    • /
    • v.42 no.10
    • /
    • pp.687-692
    • /
    • 2019
  • Transfer RNA-derived small RNAs (tsRNAs) play a role in various cellular processes. Accumulating evidence has revealed that tsRNAs are deeply implicated in human diseases, such as various cancers and neurological disorders, suggesting that tsRNAs should be investigated to develop novel therapeutic intervention. tsRNAs provide more complexity to the physiological role of transfer RNAs by repressing or activating protein synthesis with distinct mechanisms. Here, we highlight the detailed mechanism of tsRNA-mediated dual regulation in protein synthesis and discuss the necessity of novel sequencing technology to learn more about tsRNAs.

Isolation and Characterization of a Rice Mitochondrial Small Heat Shock Protein Gene

  • Kim, Do-Hyun;Alam, Iftekhar;Lee, Dong-Gi;Lee, Byung-Hyun
    • Journal of The Korean Society of Grassland and Forage Science
    • /
    • v.40 no.4
    • /
    • pp.285-290
    • /
    • 2020
  • To understand the role of small heat shock protein (sHSPs) in rice plant response to various stresses such as the heat and oxidative stresses, a cDNA encoding a 24.1 kDa mitochondrial small HSP (Oshsp24.1) was isolated from rice by rapid amplification of cDNA ends (RACE) PCR. The deduced amino acid sequence shows very high similarity with other plant small HSPs. DNA gel blot analysis suggests that the rice genome contains more than one copy of Oshsp24.1. High level of expression of Oshsp24.1 transcript was observed in rice seedlings in response to heat, methyl viologen, hydrogen peroxide, ozone, salt and heavy metal stresses. Recombinant OsHSP24.1 protein was produced in E. coli cells for biochemical assay. The protein formed oligomeric complex when incubated with Sulfo-EGS (ethylene glycol bis (succinimidyl succinate)). Our results shows that Oshsp24.1 has an important role in abiotic stress response and have potential for developing stress-tolerant plants.

Complete Nucleotide Sequence of Small Multidrug Resistance Plasmid pKH4 (Small Multidrug Resistance(smr) 플라스미드 pKH4의 염기서열 결정)

  • 고창학;문경호
    • YAKHAK HOEJI
    • /
    • v.43 no.6
    • /
    • pp.789-792
    • /
    • 1999
  • The complete nucleotide sequence of pKH4, a small multidrug resistance (smr) plasmid isolated from multidrug resistant Staphylococcus aureus SA5, was determined. Sequence analysis has revealed that pKH4 has two open reading frames for Rep and Smr proteins. The comparison of the amino acid sequence of Smr protein of pKH4 with those of other Smr proteins of various Staphylococcus showed that Smr protein of pKH4 is a new member of the SMR family.

  • PDF

A Study on the Improvement of Dietary Protein-efficiency by Supplement of the Panax Ginseng-by-products. (인삼의 부산물을 이용한 식의성 단백질의 효율 향상을 위한 연구)

  • 황우익;이성동
    • Journal of Ginseng Research
    • /
    • v.3 no.1
    • /
    • pp.1-34
    • /
    • 1979
  • Our nation is confronted with the situation that the rice, a principal food, short of some essential amino acids, leads to imbalanced meals insufficient in the nutrient of Protein, to bring many difficulties in the elevation of nutritional state in our nation. While. our country has been produced much amounts of Panax Ginseng roots which has a stimulating effects on the metabolism of protein, lipid and nucleic acids in the body. And the leaf and trunk of Panax Ginseng were also produced a considerable amounts as the by-products. Author believe that these by-products (leaf and trunk) of Panax Ginseng might have some components possessing simillar activity with Panax Ginseng root although the quantity and qualify of the functional components may more or less be different. Therefore, this study was demised to observe the supplemental effect of the Panax Ginseng-by-Products on the dietary protein efficiency and nutritional state of rats. The feeds used for this experiment were rice containing 30% barely, fish four, and the leaf, trunk and small root of the Panax Ginseng, and the contents of the general nutrients including protein, lipid and carbohydrate etc. in each feed were analyzed for the combination of each feed. And, being based on analytical values of Protein in food. fish Pour as Protein source was added were rice containing 30% barely to be include 8.6 to 8.7%, 12%, 15% and 18% of protein. Then 2% of the leaf, trunk or small reef of Panax Ginseng was supplemented into each of above protein diet group, ton 16 kinds of diets were Prepared. The male albino rats from a Pure strain, weighing 70g to 80g. were used for experimental animals. They were maintained with coresponding fist for f and 8 weeks, and the growth rate, consumption of diets and protein, efficiency of feed and Protein in animals were determined. The lipids, proteins and cholesterols in serum and liver were also determined quantitatively after they were sacrificed in coresponding term. The results obtained are summarized as follows: 1. Body weigh of diet group containing 8.6 to 8.7%,12%, and 15% of protein are increased remarkably by supplement of 2% of the leaf or small root of Panax Ginseng in comparison with each of controls. But this tendency could not observed in diet group containing 18eA Proteins. 2. Feed efficiency showed same tendency in comparison with changes of gained body weight. Specially, in each of diets containing 8.7%, 12%, 15% and 18% of Proteins, supplement of the leaf of Panax Ginseng showed the better feed efficiency than supplement of the trunk or small root. 3. In feeding group for 8 weeks, protein efficiency showed worst efficiency in diet containing 18% proteins and showed the best efficiency was the diet group containing 12% Proteins. And the efficiency was improved according to supplement of the leaf of Panax Ginseng. 4. Nitrogen contents in serum and liver did not show large differences each other in all diet groups. But contexts of total cholesterol and 1ipid were decreased markedly in diet groups containing 12%, 15% and 18% of proteins in comparison with diet group containing 8.6% to 8.8% of proteins.

  • PDF