• KSBB Journal
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• v.10 no.3
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• pp.283-291
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• 1995

The characteristics of aminopeptidase M(ApM) immobilized covalently on Cellufine Formyl and the continuous production of authentic human growth hormone(hGH) from methionyl human growth hormono(met-hGH) using the column reactor packed with immobilized ApM were investigated. Immobilized ApM with the proportion of 2.3mg ApM per 1g Cellufine Formyl gel had the highest met-hGH conversion activity. The optimum pH(7.0) and temperature($55^{\circ}C$) showed no appreciable difference between free and immobilized enzymes and the optimum temperature in continuous operation of the column reactor was also found to be $55^{\circ}C$. Under the conditions at which met-hGH was converted completely to hGH, the yield and productivity were about 77% and 0.8mg hGH/ml$.$h, respectively. In two column reactors of different sizes, met-hGH was converted to hGH with the same conversion rates and hGH yields at the same space velocities. The half-life of the reactor systems at $45^{\circ}C$ and $55^{\circ}C$ were projected from the continuous operations for 90 days to be 225 days and 81 days, respectively.

• KSBB Journal
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• v.10 no.3
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• pp.271-282
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• 1995

The authentic hGH converted from met-hGH by immobilized ApM was purified by successive chromatographic processes based on the differences in isoelectric points, hydrophobicities and charges. The final recovery yield was about 14.1% and the specific activity of the purified hGH was 2.75IU per mg when assayed by enzyme immunoassay. The purified hGH was verified to be authentic hGH through the analysis of amino acid composition, amino-terminal amino acid sequence, carboxy-terminal amino acid and tryptic peptide map. The purity of purified hGH was higher than that of commercial hGH when assessed by SDS-PAGE, PAGE, IEF and HSGF. In weight-gain assay and tibia test with hypophysectomized rats, the hGH produced in this study showed the same growth effect as the commercial hGH.

• Journal of the Korean Chemical Society
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• v.52 no.6
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• pp.608-613
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• 2008

• Korean Journal of Animal Reproduction
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• v.17 no.4
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• pp.375-383
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• 1994

The human growth hormone (hGH) gene uder the control of the rat $\beta$-casein promoter gene was designed to produce transgenic mouse expressed hGH gene in only mammary gland. One hundred seventy two eggs microinjected were transferred to the oviducts of pseudopregnants and 43 offspring were delivered. By Southern blotting hybridization, 3 were transgenic with rat $\beta$-casein/hGH gene. The copy numbers of three transgenic founder were 1, 5, and 15, respectively. A radioimmunoassay was developed to quantitate the amount of expression of the hGH gene in mammary gland of transgenic mice. The amount of hGH was 13.3ng/ml in the lactating milk of one transgenic line, showing predominantly higher than 3.0ng/ml in milk of control mice. Therefore, our findings suggested that $\beta$-casein promoter may induce the tissue specific expression of structural gene.

• Reproductive and Developmental Biology
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• v.35 no.3
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• pp.251-256
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• 2011

Human growth hormone (hGH), one of the most important hormones in medicine, is secreted from anterior pituitary gland. Its broad physiological function includes body growth, cell regeneration, increasement of muscle volume, bone density, body fat reduction, and so on. Due to the wide range of therapeutic effects, the hGH produced from E. coli has been commercialized already. In this study, we asked whether it is possible to produce recombinant hGH efficiently from various cultured mammalia cells. To meet this purpose, we chose a retrovirus vector system for transfer and expression of the hGH gene in various mammalian cells. Analyses of RT-PCR, ELISA, and Western blot to determine expression of the hGH gene showed the highest production of the hGH was determined from chicken embronic fibroblast (CEF) cells with the concentration of 8.58 ${\mu}g$/ml. The biological activity of the hGH was similar to the commercially available counterpart. These results suggest that mass production of hGH is possible not only in the E. coli but also in the various mammalian cells.

• Applied Microscopy
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• v.41 no.1
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• pp.47-53
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• 2011

Hair is an appendage of skin which protects the body from outer physical and chemical stimuli. Hair is generated from the hair follicle lying on a sunken basal layer of epidermis. Hair cycling, which regenerates hair follicles throughout the life time of the organism. Numerous kinds of factors which exist at the hair follicle have been reported to regulate hair cycling, Human growth hormone secreted from pituitary gland, initially demonstrated to accelerate organ's growth, has been reported to play a role in the biology of organ size determination. We investigated the effect of 6-histidines residues tagged at amino-terminus of human growth hormone using light and electronmicroscopic methods. Human growth hormone encapsulated in nano-liposome (LhGH) was used to find how LhGH affects hair follicle cycling of mouse (C57BL6/CrN). Distilled water as a negative control, 3% Minoxidil as a positive control, and LhGH were applied to mouse for weeks. LhGH increased the number of exposed hairs per given areas ($1mm^2$). This result was also confirmed using a different breed of mice which show natural hair loss in an old age (about 17 months after birth). When LhGH was applied for 3 weeks after natural hair loss, natural hair loss on these mice was prevented, However, the control group mice on which LhGH was not applied showed further hair loss. This result indicates that LhGH may stimulate hair cycling of mouse. In clusion, it is cleat that the LhGH increased the number of hair on mice and help the depilated skin to grow new hair follicles again.