• Journal of Science and Technology Studies
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• v.14 no.1
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• pp.87-116
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• 2014

This article focuses on synthetic hormone consumption that illegal act of heterogeneous forms of pharmaceuticalization. Athletes are not unfamiliar with the use of synthetic hormones that contain anabolic steroids. Synthetic hormones are used to increase muscle mass and strength. This drug use practice cannot simply be viewed as illegal. Athletes accumulate knowledge on these hormones that conflicts with the knowledge proffered by physicians and they consume drugs responsibly. Physicians' knowledge of these hormones is limited to their use in the treatment of abnormalities. Athletes, however, are expanding the role of these hormones to include their potential for enhancement. Thereby, a new value is assigned to synthetic hormones, and an informal market is formed. Previous studies in the fields of biopolitics and biomedicalization have mainly focused on the formal connection between biomedical science and the institutional network. This article, therefore, analyzes the informal and the various aspects of biomedicalization.

• BMB Reports
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• v.34 no.6
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• pp.502-508
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• 2001

A cDNA, encoding the human growth hormone (hGH), was synthesized based on the known 191 amino acid sequence. Its codon usage was optimized for a high level expression in Escherichia coli. Unique restriction sites were incorporated throughout the gene to facilitate mutagenesis in further studies. To minimize an initiation translation problem, a 624-bp cassette that contained a ribosome binding site and a start codon were fused to the hGH-coding sequence that was flanked between the EcoRI and HindIII sites. The whole fragment was synthesized by an overlapped extension of eight long synthetic oligonucleotides. The four-short duplexes of DNA, which were first formed by annealing and filling-in with a Klenow fragment, were assembled to form a complete hGH gene. The hGH was cloned and expressed successfully using a pET17b plasmid that contained the T7 promoter. Recombinant hGH yielded as much as 20% of the total cellular proteins. However, the majority of the protein was in the form of insoluble inclusion bodies. N-terminal amino acid sequencing also showed that the hGH produced in E. coli contained formyl-methionine. This study provides a useful model for synthesis of the gene of interest and production of recombinant proteins in E. coli.

• Asian-Australasian Journal of Animal Sciences
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• v.6 no.2
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• pp.319-323
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• 1993

The effect of bovine growth hormone digested with trypsin on whole-body protein synthesis in vitro of chicken embryos was investigated by using a whole-embryo culture system. Bovine growth hormone at 5.3 and 530 ng/ml was digested partially and completely with trypsin for 4 min and 18 h, respectively. After culturing chicken embryos with a synthetic medium containing $L-[4-^3H]$ pheylalanine, whole-embryo protein synthesis was determined from the ratio of specific radioactivities of free and protein-bound pheylalanine. Whole-embryo protein synthesis of the control group cultured with no bovine growth hormone was $49.5{\pm}2.2%/d$. There was no significant interaction between digestion time and the concentration of trypsin-digested bovine growth hormone. Tryptic digestion of bovine growth hormone increased fractional synthesis rates of whole-body protein compared to the 0-min groups, and there was no significant difference between the 4-min and 18-h groups. The higher concentration (530 ng/ml) of trypsin-digested bovine growth hormone was more effective in enhancing whole-embryo protein synthesis than the lower concentration (5.3 ng/ml).

• KOREAN JOURNAL OF CROP SCIENCE
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• v.34 no.s01
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• pp.26-32
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• 1989

The analytic principles of GC and MS were explained in relation to plant hormone analyses and the characteristics of two instruments were compared. The selection of column, condition of measurement and the method of ionization to get a good spectrum were also briefly described. Finally, the pre-treatment of sample by solvent extraction method to remove the unnecessary part of sample and the synthetic method, especially reagents and reaction condition, for the preparation of ether or ester derivative which can be easily vaporized in GC were explained.

• YAKHAK HOEJI
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• v.51 no.6
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• pp.490-494
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• 2007

TRH (thyrotropin-releasing hormone) was chemically synthesized utilizing solution phase peptide chemistry for the process development of large scaled synthesis. All the synthetic steps performed in relatively mild conditions, higher yields, easier preparations, minimum racemizations, and separation and purification by recrystallizations.

• Journal of Microbiology and Biotechnology
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• v.27 no.11
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• pp.1999-2009
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• 2017

The secretion efficiency of a protein in a Sec-type secretion system is mainly determined by an N-terminal signal peptide and its combination with its cognate protein. Five signal peptides, namely, two synthetic Sec-type and three Bacillus licheniformis alpha-amylase-derived signal peptides, were compared for periplasmic expression of the human growth hormone (hGH) in E. coli. Based on in silico predictions on the signal peptides' cleavage efficiencies and their corresponding mRNA secondary structures, a number of amino acid substitutions and silent mutations were considered in the modified signal sequences. The two synthetic signal peptides, specifically designed for hGH secretion in E. coli, differ in their N-terminal positively charged residues and hydrophobic region lengths. According to the mRNA secondary structure predictions, combinations of the protein and each of the five signal sequences could lead to different outcomes, especially when accessibility of the initiator ATG and ribosome binding sites were considered. In the experimental stage, the two synthetic signal peptides displayed complete processing and resulted in efficient secretion of the mature hGH in periplasmic regions, as was demonstrated by protein analysis. The three alpha-amylase-derived signal peptides, however, were processed partially from their precursors. Therefore, to achieve efficient secretion of a protein in a heterologous system, designing a specific signal peptide by using a combined approach of optimizations of the mRNA secondary structure and the signal peptide H-domain and cleavage site is recommended.

• Asian-Australasian Journal of Animal Sciences
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• v.15 no.5
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• pp.757-766
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• 2002

Growth hormone-releasing peptide-2 (GHRP-2, also named KP102) is a new hexapeptide of a series of synthetic growth hormone-releasing peptides (GHRPs) which stimulates the secretion of growth hormone (GH) in vitro and in vivo in several species including calf, sheep and pig. The GH-releasing activity of GHRP-2 is two to three times more effective than that of the original GHRP-6, and GHRP-1 in the rats and humans. To date, GHRP-2 seems to be the most potent member of the family of GHRPs. Since the GHRPs are short peptides (5-7 amino acid residues), they are synthesized easily and are not as readily degraded in plasma as GHreleasing hormone (GHRH). These features ameliorate their potential on domestic animals because of their chemical nature the GHRPs are efficacious when administered i.v. orally or orally. However, studies in cow, pig and sheep do not indicate such a close relationship between GHRH, somatostatin (SS) and GH, calling into question the general applicability of the human and rat models. Perhaps there is an important role for an endogenous GHRP in the regulation of GH secretion in domestic animals. This review provides an overview on the current knowledge of physiological role of GHRP-2 in domestic animals.

• 대한핵의학회:학술대회논문집
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• 1975.06a
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• pp.77.1-77.1
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• 1975

• Biomedical Science Letters
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• v.15 no.3
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• pp.249-255
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• 2009

All living things have been developed efficient strategies to cope with external and internal environmental changes via a process termed 'homeostasis'. However, chronic prenatal maternal stress may significantly contributes to pregnancy complications by disturbing hypothalamic-pituitary-adrenal (HPA) axis and the automatic nervous system (ANS), and results in unfavorable development of the fetus. Dysregulation of these two major stress response systems lead to the increased secretion of the glucocorticoids (GCs) which are known to be essential for normal development and the maturation of the central nervous system. As Hox genes are master key regulators of the embryonic morphogenesis and cell differentiation, we aimed to determine the effects of dexamethasone, a potent synthetic glucocorticoid, on gene expression in mesenchymal stem cell C3H10T1/2. Analysis of 39 Hox genes based on reverse transcription PCR (RT-PCR) method revealed that the expression patterns of Hox genes were overall upregulated by long dexametasone treatment. These results indicate that maternal stress may have a deleterious effect on early developing embryo through the stress hormone, glucocorticoid.

• Journal of Life Science
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• v.28 no.3
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• pp.284-292
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• 2018

The melanin-concentrating hormone (MCH), a cyclic hypothalamic peptide composed of 17 amino acids, was initially identified in chum salmon (Oncorhynchus keta) as a regulator of pigmentation. Mammalian MCHs are cyclic hypothalamic peptides composed of 19 amino acids that regulate food intake and energy homeostasis. The present study examined not only MCH expression of different tissues but also the melanohore aggregation and intracellular $Ca^{2+}$ influx of fMCH and the other MCH. Real-time qPCR showed that MCH expressed specially in the brain, gonad, and ovary, and expression of MCH was observed during the developmental stages. In the application of synthetic fMCH and both types of synthetic fMCH, dN-fMCH and dC-fMCH, scale melanophore induced significant changes in aggregation activity with various concentrations of MCH. Also, compared to hMCH and sMCH, fMCH exhibited a 36~99.85% increase in relative potency (%), whereas aggregation of dN-fMCH and dC-fMCH remained in a high concentration. However, dispersion was induced rapidly according to be low concentration of dN-fMCH and dC-fMCH. We show that fMCH and its derivates were bound human MCHR1 and rat MCHR expressed in HEK293T cells with nano-molar affinity and are likely to be ligand-induced to mobilize intracellular $Ca^{2+}$. These results may provide new ligands for binding assay with MCHew ligands, as a structure similar to the mammalian MCH structure was discovered in fish. Once the fMCH receptor system is in place, it can be compared to the MCH system of mammals in terms of MCH function.