• Parasites, Hosts and Diseases
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• 제42권3호
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• pp.141-143
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• 2004

After collecting calcareous corpuscles from plerocercoid of Spirometra mansoni (sparganum), we evaluated the antigenic values of calcareous corpuscles binding proteins obtained from the cyst fluid of Taenia solium metacestodes. Immunoblot analysis revealed that cysticercosis patient sera strongly recognized 10 and 95 kDa calcareous corpuscles binding proteins. This result demonstrated that calcareous corpuscles are bound with major secretory antigenic proteins, which is possibly involved in the secretory pathways of the 10 and 95 kDa proteins presenting in the cyst fluid of T. solium metacestodes.

• 한국작물학회:학술대회논문집
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• 한국작물학회 2017년도 9th Asian Crop Science Association conference
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• pp.129-129
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• 2017

The first key point to the successful pollination and fertilization in plants is the pollen pistil interaction, referring to the cellular and molecular levels, which mainly play active roles in limiting gene flow among maize populations and between maize and teosinte. This study was carried out to identify proteins and investigate the mechanism of gametophytic factors using protein analysis. W22 (ga1); which didn't carry a gametophytic factor and W22 (Ga1), a near iso-genic line were used for the proteome investigation. SDS-PAGE was executed to investigate proteins in the pollen and pistil of W22 (ga1) and W22 (Ga1). A total of 44 differentially expressed proteins were identified in the pollen and pistil on SDS-PAGE using LTQ-FTICR MS. Among the 44 proteins, a total of 24 proteins were identified in the pollen of W22 (ga1) and W22 (Ga1) whereas 20 differentially expressed proteins were identified from the pistil of W22 (Ga) and W22 (Ga1). However, in pollen, 2 proteins were identified only in the W22 (ga1) and 12 proteins only in the W22 (Ga1) whereas 10 proteins were confirmed from the both of W22 (ga1) and W22 (Ga1). In contrary, 10 proteins were appeared only in the pistil of W22 (ga1) and 7 proteins from W22 (Ga1) while 3 proteins confirmed in the both of W22 (ga1) and W22 (Ga1). Moreover, the identified proteins were generally involved in hydrolase activity, nucleic acid binding and nucleotide binding. These results help to reveal the mechanism of gametophytic factors and provide a valuable clue for the pollen and pistil research in maize. In addition, it might provide a comprehensive insight on the proteins that were involved in the regulation of pollen-pistil interaction.

• 한국응용약물학회:학술대회논문집
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• 한국응용약물학회 2002년도 창립10주년기념 및 국립독성연구원 의약품동등성평가부서 신설기념 국재학술대회:생물학적 동등성과 의약품 개발 전략을 위한 국제심포지움
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• pp.113-113
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• 2002

Phylogenetically conserved Bcl-2 family proteins play a pivotal role in the regulation of apoptosis from virus to human. Members of the Bcl-2 family consist of antiapoptotic proteins such as Bcl-2, Bcl-xL, and Bcl-w, and proapoptotic proteins such as BAD, Bax, BOD, and Bok. It has been proposed that anti- and proapoptotic Bcl-2 proteins regulate cell death by binding to each other and forming heterodimers. A delicate balance between anti- and proapoptotic Bcl-2 family members exists in each cell and the relative concentration of these two groups of proteins determines whether the cell survives or undergoes apoptosis. Mcl-1 (Myeloid cell :leukemia-1) is a member of the Bcl-2 family proteins and was originally cloned as a differentiation-induced early gene that was activated in the human myeloblastic leukemia cell line, ML-1 . Mcl-1 is expressed in a wide variety of tissues and cells including neoplastic ones. We recently identified a short splicing variant of Mcl-1 short (Mcl-IS) and designated the known Mcl-1 as Mcl-1 long (Mcl-lL). Mcl-lL protein exhibits antiapoptotic activity and possesses the BH (Bcl-2 homology) 1, BH2, BH3, and transmembrane (TM) domains found in related Bcl-2 proteins. In contrast, Mcl-1 S is a BH3 domain-only proapoptotic protein that heterodimerizes with Mcl-lL. Although both Mc1-lL and Mcl-lS proteins contain BH domains fecund in other Bcl-2 family proteins, they are distinguished by their unusually long N-terminal sequences containing PEST (proline, glutamic acid, serine, and threonine) motifs, four pairs of arginine residues, and alanine- and glycine-rich regions. In addition, the expression pattern of Mcl-1 protein is different from that of Bcl-2 suggesting a unique role (or Mcl-1 in apoptosis regulation. Tankyrasel (TRF1-interacting, ankyrin-related ADP-related polymerasel) was originally isolated based on its binding to TRF 1 (telomeric repeat binding factor-1) and contains the sterile alpha motif (SAM) module, 24 ankyrin (ANK) repeats, and the catalytic domain of poly(adenosine diphosphate-ribose) polymerase (PARP). Previous studies showed that tankyrasel promotes telomere elongation in human cells presumably by inhibiting TRFI though its poly(ADP-ribosyl)action by tankyrasel . In addition, tankyrasel poly(ADP-ribosyl)ates Insulin-responsive amino peptidase (IRAP), a resident protein of GLUT4 vesicles, and insulin stimulates the PARP activity of tankyrase1 through its phosphorylation by mitogen-activated protein kinase (MAPK). ADP-ribosylation is a posttranslational modification that usually results in a loss of protein activity presumably by enhancing protein turnover. However, little information is available regarding the physiological function(s) of tankyrase1 other than as a PARP enzyme. In the present study, we found tankyrasel as a specific-binding protein of Mcl-1 Overexpression of tankyrasel led to the inhibition of both the apoptotic activity of Mel-lS and the survival action of Mcl-lL in mammalian cells. Unlike other known tankyrasel-interacting proteins, tankyrasel did not poly(ADP-ribosyl)ate either of the Mcl-1 proteins despite its ability to decrease Mcl-1 proteins expression following coexpression. Therefore, this study provides a novel mechanism to regulate Mcl-1-modulated apoptosis in which tankyrasel downregulates the expression of Mcl-1 proteins without the involvement of its ADP-ribosylation activity.

• 한국작물학회지
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• 제58권4호
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• pp.388-392
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• 2013

The proteins from functional rice cultivars (Nogwonchalbyeo, Giant embryonic, Arhyangchalbyeo, and Goamibyeo) and general white rice were extracted and separated using two-dimensional (2D) gel electrophoresis. A wide variation in the molecular weight (MW) and pH range of the expressed proteins in rice samples were observed. The green-kerneled rice (Nogwonchalbyeo) exhibited proteins with MW of 9-57 kDa and appeared at a pH range of 4-7. The Giant embryonic contained proteins with MW of 31-63 kDa and a pH range of 5-6. The aromatic glutinous rice (Arhyangchalbyeo) showed proteins with MW of 24-28 and pH of 5.8-6.8. The high-amylose rice (Goamibyeo) exhibited proteins with MW of 3-63 and pH of 5.2-5.6. The identified proteins uniquely found and highly expressed in each cultivar may have a significant role on rice functionality. The results illustrate that the 2D gel electrophoresis is a valuable method in the determination of the protein expression profiles in functional rice grains and may be useful in the identification of specific marker proteins associated with the functional property of rice.

• 한국동물학회지
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• 제23권1호
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• pp.1-12
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• 1980

큐티클 形成 및 硬化過程中 血蛋白質의 變化와 起源을 규명하고자 acrylamide gel electrophoresis와 immunodiffusion 方法을 使用하였다. Acrylamide gel electrophoresis에서 적어도 19개의 protein band가 혈림프에서 發見되었으며 脂肪體에서는 13개의 band가 確認되었는데 이들은 대체적으로 일정한 pattern을 유지하였다. 또한 혈림프와 脂肪體의 一般的인 protein band의 pattern은 $3\\sim4$개의 강하게 染色된 band와 몇 개의 가는 band가 gel의 상단에 存在하는 것이 특징이었고 적어도 5개 이상의 haemolymph protein band가 　期初에 걸쳐 일정하게 나타났다. Immunodiffusion test에서는 $8\\sim9$개의 血蛋白質에 　期初에서 나타났는데 그중 2개의 血蛋白質은 　期前에 나타났으며 다른 두 血蛋白質도 　化직 후 脂肪體에서 나타남으로써 脂肪體가 이들 血蛋白質의 起源임을 암시하였다.

• BMB Reports
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• 제32권5호
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• pp.497-501
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• 1999

Biotinylation of recombinant proteins is a powerful tool for the detection and analysis of proteins of interest in a large variety of assay systems. The recent development of in vivo biotinylation techniques in E. coli has opened new possibilities for the production of site-specifically biotinylated proteins without the need for further manipulation after the isolation of the recombinantly expressed proteins. In the present study, a novel vector set was generated which allows the convenient cloning and expression of proteins of interest fused with an N-terminal in vivo biotinylated thioredoxin (TRX) protein. These vectors were derived from the previously reported pBIOTRX vector into which was incorporated part of the pBluescript II+phagemid multiple cloning site (MCS), amplified by PCR using a pair of sophisticated oligonucleotide primers. The functionality of these novel vectors was examined in this system by recombinant expression of rat transforming growth factor-$\beta$. Western-blot analysis using TRX-specific antibodies or peroxidase-conjugated streptavidin confirmed the successful induction of the fusion protein and the in vivo conjugation of biotin molecules, respectively. The convenience of molecular subcloning provided by the MCS and the effective in vivo biotinylation of proteins of interest makes this novel vector set an interesting alternative for the production of biotinylated proteins.

• The Plant Pathology Journal
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• 제33권6호
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• pp.614-618
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• 2017

The root-knot nematode Meloidogyne incognita infects a variety of plants, including Arabidopsis thaliana. During migration, root-knot nematodes secrete different proteins to modify cell walls, which include pectolytic enzymes. However, the contribution of host cell wall proteins has not been described during this process. The function of two DUF642 cell wall proteins, BIIDXI (BDX, At4g32460) and TEEBE (TEB, At2g41800), in plant development could be related to the regulation of pectin methyl esterification status in the cell walls of different tissues. Accordingly, the expression of these two genes is up-regulated by auxin. BDX and TEB were highly induced during early M. incognita inoculation. Moreover, cell wall localization of the proteins was also induced. The cell wall localization of BDX and TEB DUF642 proteins during M. incognita early inoculation suggested that these two proteins could be involved in the regulation of the degree of pectin methylation during cell separation.

• 한국식품영양과학회지
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• 제30권3호
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• pp.505-509
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• 2001

This study was carried out to evaluate the application of food irradiation technology as a method for reducing milk allergies. Bovine $\alpha$-casein, $\beta$-casein, $textsc{k}$-casein, $\alpha$-lactalbumin(ALA), $\beta$-lactoglobulin (BLG) and serum albumin (BSA) were used as model allergens of milk proteins and the proten solution (2.0 mg/mL) with 0.01 M phosphate buffered saline (pH 7.4) was irradiated at 3, 5 and 10 kGy. Using milk-hypersensitive patients IgE (MHP-IgE), the changes of binding ability to irradiated proteins were observed by competitive indirect enzyme-linked immunosorbent assay (Ci-ELISA). Affinity of MHP-IgE to milk proteins was higher in ALA and BLG than that of other proteins. Standard curve to each non-irradiated protein could be made with MHP-IgE for quantifying milk allergens. Binding abilities of MHP-IgE to the irradiated proteins, however, decreased with different slopes of the standard curves. Sensitivity of gamma irradiation was higher in ALA and BLG than of other proteins. These results indicated that irradiation technology can be used to reduce the milk hypersensitivity.

• 한국작물학회:학술대회논문집
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• 한국작물학회 2017년도 9th Asian Crop Science Association conference
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• pp.86-86
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• 2017

Prolamins are the main seed storage proteins in cereals. Gluten proteins seem to be prolamins because their primary structure have the meaningful quantity of proline and glutamine amino acid residues. Gluten proteins are found in crops such as wheat (Triticum aestivum), barley (Hordeum vulgare), and rye (Secale cereale) which are major food crops in the Triticeae tribe. Glutenin and gliadin, hordein, and secalin are typical gluten proteins found in wheat, barley, and rye, respectively. Gluten affect grain quality so that many researches, such as isolation or characterization of their genes, have been carried out. To improve the quality of grains in the Triticeae tribe, it is necessary to understand the relationship within their gluten proteins and their evolutionary changes. The sequences of nucleotides and amino acids of gluten protein including glutenins, gliadins, hordeins, and secalins were retrieved from NCBI (https://www.ncbi.nlm.nih.gov/) and Uniprot (http://www.uniprot.org/). The sequence analysis and the phylogenetic analysis of gluten proteins were performed with various website tools. The results demonstrated that gluten proteins were grouped with their homology and were mostly corresponded with the previous reports. However, some genes were moved, duplicated, or disappeared as evolutionary process. The obtained data will encourage the breeding programs of wheat, barley, rye, and other crops in the Triticeae tribe.

• Asian-Australasian Journal of Animal Sciences
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• 제14권12호
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• pp.1678-1682
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• 2001

The total proteins were estimated in both deoxycholate (DOC)-extract of sperm membrane and seminal plasma of chilled as well as frozen semen obtained from five Murrah buffalo bulls. Proteins were further characterized by polyacrylamide gel electrophoresis (PAGE) in three bulls. The protein content of sperm membrane extract (SME) and that of seminal plasma (SP) decreased gradually with increase in freezing period from 6 to 24 mo when compared with the values observed in freshly chilled semen in all bulls. The total decrease in protein content of SME and SP varied from 30-40% and 28-59% respectively during 6-24 mo of freezing. The number of glycoproteins/proteins (GP/P) in SME varied from 4-8 in freshly-chilled semen of all bulls and reduced to 2-4 after 24 mo of freezing. In SP, the number of proteins varied from 6-10 in freshly chilled semen of all bulls and reduced to 3-8 after 24 mo of freezing. Some of the proteins in SME and SP disappeared, others got altered and appeared with change in molecular weight after different freezing times. These studies reveal that alterations in the sperm membrane proteins may be responsible for damage to their membrane during freezing and thus lowering their fertilizability.