• Journal of the Korea Academia-Industrial cooperation Society
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• v.4 no.3
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• pp.230-235
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• 2003

수용성, 구형의 단백질 분자는 기능성(효소, 유화제, 중화제 등)에 따라 센서나 유사생체기관에 응용성이 크다. 본 연구는 물-공기 계면에서 형성되는 단백질의 표면상태방정식(일명 표면등온선)을 이론적으로 도출하고 그 결과를 실험적으로 확인하여 단백질 분자의 기능적 이용에 활용하고자 한 것이다. 아미노산 부분사슬간, 분자와 물과의 인력, 정전기적 인력을 고려하여 종합적 상태방정식을 도출하였으며 탄소 14로 tagging한 albumin실험과 비교하여 상당히 일치하는 경향을 확인할 수 있었다.

• Journal of Microbiology and Biotechnology
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• v.17 no.10
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• pp.1695-1699
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• 2007

Ferritin is an iron storage protein found in most living organisms as a natural assembled macromolecule. For studying the functional ability of the ferritin assembly, human H- and L-ferritins were expressed and purified from Pichia pastoris strain GS115. The recombinant H- and L-ferritins showed a globular form with transmission electron microscopy. The rate of iron uptake for H-ferritin was significantly faster than that for the L-ferritin in vitro. By gel permeation chromatography analysis, recombinant ferritins were confirmed as multimeric subunits with high molecular weight and it was indicated that assembled subunits were able to store iron in vivo.

• BMB Reports
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• v.41 no.1
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• pp.35-40
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• 2008

The molten globular conformation of V26A ubiquitin (valine to alanine mutation at residue 26) was studied by nuclear magnetic resonance spectroscopy in conjunction with amide hydrogen/deuterium exchange. Most of the amide protons that are involved in the native secondary structures were observed to be protected in the molten globule state with the protection factors from 1.2 to 6.7. These protection factors are about 2 to 6 orders of magnitude smaller than those of the native state. These observations indicate that V26A molten globule has native-like backbone structure with marginal stability. The comparison of amide protection factors of V26A ubiquitin molten globule state with those of initial collapsed state of the wild type ubiquitin suggests that V26A ubiquitin molten globule state is located close to unfolded state in the folding reaction coordinate. It is considered that V26A ubiquitin molten globule is useful model to study early events in protein folding reaction.

• Bulletin of the Korean Chemical Society
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• v.20 no.9
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• pp.999-1004
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• 1999

Two compact sized globular proteins, β-lactoglobulin and α-lactalbumin were kinetically characterized at the aqueous solution surface with the measurement of surface pressure (π) and surface concentration (Γ) via a radiotracer method. The adsorption kinetics was of diffusion control at early times, the rates of increase of πand Γ being lower at longer times due to growing energy barrier. At low concentrations, an apparent time lag was observed in the evolution of π for β-lactoglobulin but not for α-lactalbumin which was shown to be due to the non-linear nature of the p- G relationship for the former. The area per molecule of an adsorbed β-lactoglobulin during adsorption was smaller than that for spread monolayer since β-lactoglobulin was not fully unfolded during the adsorption. For α-lactalbumin, however, no such difference in the molecular areas for adsorbed and spread monolayer was observed indicating thereby that α-lactalbumin unfolded much more rapidly (has looser tertiary structure) than β-lactoglobulin. Surface excess concentrations of α-lactalbumin was found to evolve in two steps possibly due to the change in the orientation of the adsorbed protein from a side-on to an end-on orientation.

• Proceedings of the PSK Conference
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• 2003.10b
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• pp.145.3-146
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• 2003

Transgenic Eleutherococcus senticosus plants were prepared by introducing the genes for squalene synthase (SQS), hygromycin phosphotransferase (HPT) and green fluorescent Protein (GFP) through Agrobacterium-mediated transformation. The enzyme, SQS, represents a putative branch point in the isoprenoid pathway capable of diverting carbon flow specifically to the biosynthesis of phytosterol and oleanolic acid. The full SQS gene was isolated from P. ginseng roots. Early globular embryo clusters developed from embryogenic callus were used as the explant source. (omitted)

• The Korean Journal of Zoology
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• v.31 no.1
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• pp.62-70
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• 1988

The distribution of respiratory chain complexes in beef heart and human muscle mitochondria has been explored by immunoeledron microscopy with antibodies made against beef heart mltochondriai proteins in conjundion with protein A cofloidai gold (l2nm particles). The antibodies used were made against NADH-conezyme Q reductase(complex I), ubiquinol-cytochrome-c-oxldoreductase (complex III) and cytochrome-c-oxidase(complex IV). Labeling of bed heart tissue with any of these antihodies gave gold particles randomly distributed along the mitochondrial inner membrane. The labeling of muscle tIssue mitochondria from a patient with a mitochondrial myopathy localized by biochemical analysis to complex III was quantitated and compared with the labeling of human control muscle tissue mitochondria. Four kinds of morphological changes in the mitochondrial fine strudure in the myopathy patient tissue have been found; paracrystalline inclusions consistIng of densely packed multi- lamellar structures, globular crystalline inclusions with high electron density, multilamellar strudure inclusion body(compadly and irregularly arranged concentric whirl shaped cristae)and golbular cyrstalilne inclusions located in the center of the whirl shaped cristae. Compex I and cytochrome-c-oxldase antihodies reacted to the same level in the mitochondria containing the crystalline inclusions and control mitochondria. Antibodies to complex III reacted very poorly to the mitochondria containing the crystalline Inclusions but strongly to control mitchondria. The globular crystalline inclusions in the mitochondria are not reacted antibodies to respiratory chain complexes.

• Food Science of Animal Resources
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• v.36 no.2
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• pp.267-274
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• 2016

The purposes of this study were to investigate the impacts of concentration levels of whey protein isolate (WPI) and inulin on the formation and physicochemical properties of WPI/inulin nano complexes and to evaluate their potential prebiotic effects. WPI/inulin nano complexes were produced using the internal gelation method. Transmission electron microscopy (TEM) and particle size analyzer were used to assess the morphological and physicochemical characterizations of nano complexes, respectively. The encapsulation efficiency of resveratrol in nano complexes was studied using HPLC while the potential prebiotic effects were investigated by measuring the viability of probiotics. In TEM micrographs, the globular forms of nano complexes in the range of 10 and 100 nm were successfully manufactured. An increase in WPI concentration level from 1 to 3% (w/v) resulted in a significant (p<0.05) decrease in the size of nano complexs while inulin concentration level did not affect the size of nano complexes. The polydispersity index of nano complexes was below 0.3 in all cases while the zeta-potential values in the range of -2 and -12 mV were observed. The encapsulation efficiency of resveratrol was significantly (p<0.05) increased as WPI and inulin concentration levels were increased from 1 to 3% (w/v). During incubation at 37℃ for 24 h, WPI/inulin nano complexes exhibited similar viability of probiotics with free inulin and had significantly (p<0.05) higher viability than negative control. In conclusions, WPI and inulin concentration levels were key factors affecting the physicochemical properties of WPI/inulin nano complexes and had potential prebiotic effect.

• Nuclear Engineering and Technology
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• v.52 no.10
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• pp.2320-2327
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• 2020

The extreme hydrophobicity of expanded polytetrafluoroethylene (ePTFE) hinders bone-tissue integration, thus limiting the use of ePTFE in medical implant applications. To improve the potential of ePTFE as a biomaterial, 2-hydroxyethyl methacrylate (HEMA) was grafted onto the ePTFE surface using the gamma irradiation technique. The characteristics of the grafted ePTFE were successfully evaluated using attenuated total reflectance Fourier transform infrared (ATR-FTIR), field-emission scanning electron microscopy (FESEM)/energy dispersive X-ray (EDX), and X-ray photoelectron spectroscopy (XPS). Under the tensile test, the modified ePTFE was found to be more brittle and rigid than the untreated sample. In addition, the grafted ePTFE was less hydrophobic with a higher percentage of water uptake compared to the untreated ePTFE. The protein adsorption test showed that grafted ePTFE could adsorb protein, which was denoted by the presence of N peaks in the XPS analysis. Moreover, the formation of the globular mineral on the grafted ePTFE surface was successfully visualized using the FESEM analysis, with a ratio of 1.94 for Ca:P minerals by the EDX. To summarize, the capability of the modified ePTFE to show protein adsorption and mineralization indicates the improvement of the polymer properties, and it can potentially be used as a biomaterial for implant application.

• Reproductive and Developmental Biology
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• v.37 no.4
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• pp.169-174
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• 2013

Sperm capacitation refers to polymerization of filamentous (F)-actin from globular (G)-actin. While the role of actin-related protein 2/3 (Arp2/3) complex in actin polymerization is well appreciated, the underlying mechanism(s) and its relationship with capacitation are poorly understood. Therefore, to evaluate the potential role of Arp2/3 complex on capacitation, bovine spermatozoa were incubated with multiple doses (1, 10 and $100{\mu}M$) of CK-636, an inhibitor of Arp2/3 complex with heparin. The cellular localization of the Arp2/3 complex in spermatozoa was identified by immunohistochemistry, whereas western blot was also applied to detect the protein tyrosine phosphorylation of sperm proteins. Additionally, sperm motility and kinematic parameters were evaluated using a computer-assisted sperm analysis system. CK-636 resulted in significant changes in the ratio of Arp2/3 complex localization between acrosome and equatorial region of the spermatozoa. Short-term exposure of spermatozoa to $100{\mu}M$ of CK-636 significantly decreased sperm motility, however a non-detectable effect on protein tyrosine phosphorylation was observed during capacitation. On the basis of these results, we propose that Arp2/3 complex is associated with morphological changes during capacitation and compromised sperm motility.

• Korean Journal of Plant Tissue Culture
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• v.21 no.1
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• pp.15-22
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• 1994

To understand the molecular mechanism of hardening process in somatic embryo development and artificial seed germination in celery (Apium graveolens L.), the changes of protein synthesis by ABA or cold teatment at early globular stage were examined. Protein content and nitrate reductase activity in ABA- or cold-treated somatic embryo and seedlings were higher than that in unheated ones. The protein content and nitrate reductase activity were more prominent in somatic embryos than in seedlings. From two-dimensional electrophoresis, several protein spots specific to ABA or cold treatment were identified: 30 KD, 32 KD, 171 KD and 205 KD at heart-shaped stage; and 29 KD, 33 KD, 37 KD, 38 KD, 41 KD, 55 KD, 66 KD, and 110 KD at cotyledonary stage were the most specifically synthesized However the synthesis of certain polypeptides were repressed at heart-shaped or cotyledonary stage: 42 KD, 44 KD, 59 KD, 64 KD, 101 KD, 104 KD, and 190 KD at heart-shaped stage; and 29 KD and 116 KD at cotyledonary stage. The protein pattern changes by ABA or cold treatment occurred simultaneously and mainly in acid-soluble proteins during somatic embryo development and artificial seed germination. Therefore it is suggested that the metabolic changes for adaptation to environmental change occur during somatic embryo development and the germination and growth of seedling from embryo.