• Parasites, Hosts and Diseases
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• v.33 no.2
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• pp.101-106
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• 1995

Soluble protein of purified Pneumocvstis cnrinii was prepared from experimentally infected rats. SDS-PAGE of the crude antigen resolved about 20 protein bands from 20 to 200 kDa. Out of thenl, 116 kDa band strongly reacted and 45-55 and 100 kDa bands reacted weakly to the positive reference human serum from U.S.A. Western blot analysis with sera of 130 normal children and 15 newborns in Korea revealed specific IgG antibody reaction to 40-55 and 116 kDa protein bands. Forty percent (40.0%) of the 145 sera were positive with any of the antigenic protein bands of R corinii. The positive rate was 56% in 50 males and 33.3% in 48 females. The protein bands 40-55 and 116 kDa from rat P. carinii were confirmed to cross-react with human sera in Korea.

• Parasites, Hosts and Diseases
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• v.28 no.2
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• pp.101-108
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• 1990

Surgically collected cystic fluid of Taenia solium metacestodes from patients of intracranial cystic lesion were compared in their protein composition with those from naturally infected pigs in Cheju Do, Korea and Ecuador. In non-denaturing discontinuous-polyacryla aide gel electrophoresis (disc-PAGE) , no discernible differences were recognized in banding patterns between the cystic fluids from Cheju Do and Ecuador, and between the cystic quids from pigs and human lesions except wider bands that corresponded to human albumin and T-globulin (in 4 of 9 patients). In reducing SDS-PAGE, bands in the cystic Ruid from Ecuador showed the same banding pattern with that from Cheju Do but two bands of 21 and 17 kDa were stained darker. Cystic quids (rom patients revealed the same protein compositions of the major protein bands of 94, 64, 15, 10 and 7 kDa as in the cystic fluid of pig origin, but human albumin (66 kDa), heavy and light chains of gamma globulin (55 and 22.5 kDa) were contaminated in 4 of 9 cystic fluids. Human CSF proteins seem to have been contaminated during cystic ftuid collection. In any cystic quid from patients, the majcr Protein component was 150 kDa which was subdivided into 15, 10 and 7 kDa in reducing SDS-PAGE.

• Proceedings of the Korean Society for Food Science of Animal Resources Conference
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• 2004.10a
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• pp.375-379
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• 2004

Probiotic 활성이 높은 L. acidophilus 30SC의 생존성을 증진시키기 위한 기초자료를 얻고자, 열처리 동안 새로이 발현되는 단백질을 일차원 및 이차원 전기영동을 이용하여 확인하였으며, 세포 모양을 주사전자현미경을 사용하여 관찰하였다. $55^{\circ}C$의 heat shock에는 L. acidphilus 30SC의 사멸이 있는 것으로 나타났다. 나머지 처리구는 $37^{\circ}C$에서 계속 배양한 것과 별다른 차이를 나타내지 않았다. $45^{\circ}C$로 heat shock을 준 경우 $37^{\circ}C$에서 배양한 것과 거의 동일하였다. $55^{\circ}C$에서 15분 heat shock을 준 경우 약 22kDa와 25kDa의 단백질들이 새로이 발현된 것으로 나타났으나, 24 kDa와 27kDa로 추정되는 단백질의 발현정도는 낮았음을 확인하였다. 이차원 전기영동을 실시한 결과, $37^{\circ}C$와 비교할 때 $55^{\circ}C$로 heat shock을 준 경우 새로이 5개의 protein spot을 발견할 수 있었다. 그러나 6개의 단백질 spot은 $55^{\circ}C$ heat shock에서 소실된 것으로 확인되어 추가적인 단백질의 분석이 필요한 것으로 생각되었다.

• Journal of Life Science
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• v.18 no.9
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• pp.1219-1224
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• 2008

The embryonic zebrafish (Danio rerio) is rapidly becoming an important model organism for studies of early events in vertebrate development. Neural crest-derived pigment cell precursors of the embryonic zebrafish give rise to melanophores, xanthophores, and/or iridophores. Cell-signaling mechanisms related to the development of pigmentation and pigment pattern formation remain obscure. In this study, zebrafish embryos were treated with various signaling-related molecules - LiCl (an inositol-phosphatase inhibitor), forskolin (a protein kinase-A activator), a combination of LiCl/forskolin, and LiCl/heparin (an IP3 inhibitor) in order to identify the mechanisms involved in pigmentation. LiCl treatment resulted in ultrastructural and morphological alterations of melanophores. To identify the possible proteins responsible for this ultrastructural and morphological change, phosphorylation patterns in vitro and in vivo were analyzed. LiCl and LiCl/forskolin treatment elicited dramatic increases in the phosphorylation of a 55-kDa protein which was inhibited by heparin treatment. LiCl treatment also induced phosphorylation of a 55-kDa protein in melanophores purified from adult zebrafish. Collectively these results suggest that a LiCl-induced 55-kDa phosphoprotein plays a role in melanophore morphology and ultrastructure and ultimately effects gross pigmentation.

• Proceedings of the Botanical Society of Korea Conference
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• 1999.07a
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• pp.57-62
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• 1999

Light-regulated translation of chloroplast mRNAs requires nuclear-encoded trans-acting factors that interact with the 5' untranslated region (UTR) of these mRNAs. A set of four proteins (60, 55, 47, and 38 kDa) that bind to the 5'-UTR of the psbA mRNA had been identified in C. reinhardtii. 47 kDa protein (RB47) was found to encode a chloroplast poly (A)-binding protein (cPABP) that specifically binds to the 5'-UTR of the psbA mRNA, and essential for translation of this mRNA, cDNA encoding 60 kDa protein (RB60) was isolated, and the amino acid sequence of the encoded protein was highly homologous to plants and mammalian protein disulfide isomerases (PDI), normally found in the endoplasmic reticulum (ER). Immunoblot analysis of C. reinhardtii proteins showed that anti-PDI recognized a distinct protein of 56 kDa in whole cell extract, whereas anti-rRB60 detected a 60 kDa protein. The ER-PDI was not retained on heparin-agarose resin whereas RB60 was retained. In vitro translation products of the RB60 cDNA can be transported into C. reinhardtii chloroplast in vitro. Immunoblot analysis of isolated pea chloroplasts indicated that higher plant also possess a RB60 homolog. In vitro RNA-binding studies showed that RB60 modulates the binding of cPABP to the 5'-UTR of the psbA mRNA by reversibly changing the redox status of cPABP using redox potential or ADP-dependent phosphorylation. Site-directed mutagenesis of -CGHC- catalytic site in thioredoxin-like domain of RB60 is an unique PDI located in the chloroplast of C. reinhardtii, and suggest that the chloroplast PDI may have evolved to utilize the redox-regulated thioredoxin like domain as a mechanism for regulating the light-activated translation of the psbA mRNA.

• Proceedings of the Botanical Society of Korea Conference
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• 1985.08b
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• pp.7-18
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• 1985

Light-regulated translation of chloroplast mRNAs requires nuclear-encoded trans-acting factors that interact with the 5' untranslated region (UTR) of these mRNAs. A set of four proteins (60, 55, 47, and 38 kDa) that bind to the 5'-UTR of the psbA mRNA had been identified in C. reinhardtii. 47 kDa protein (RB47) was found to encode a chloroplast poly (A)-binding protein (cPABP) that specifically binds to the 5'-UTR of the psbA mRNA, and essential for translation of this mRNA, cDNA encoding 60 kDa protein (RB60) was isolated, and the amino acid sequence of the encoded protein was highly homologous to plants and mammalian protein disulfide isomerases (PDI), normally found in the endoplasmic reticulum (ER). Immunoblot analysis of C. reinhardtii proteins showed that anti-PDI recognized a distinct protein of 56 kDa in whole cell extract, whereas anti-rRB60 detected a 60 kDa protein. The ER-PDI was not retained on heparin-agarose resin whereas RB60 was retained. In vitro translation products of the RB60 cDNA can be transported into C. reinhardtii chloroplast in vitro. Immunoblot analysis of isolated pea chloroplasts indicated that higher plant also possess a RB60 homolog. In vitro RNA-binding studies showed that RB60 modulates the binding of cPABP to the 5'-UTR of the psbA mRNA by reversibly changing the redox status of cPABP using redox potential or ADP-dependent phosphorylation. Site-directed mutagenesis of -CGHC- catalytic site in thioredoxin-like domain of RB60 is an unique PDI located in the chloroplast of C. reinhardtii, and suggest that the chloroplast PDI may have evolved to utilize the redox-regulated thioredoxin like domain as a mechanism for regulating the light-activated translation of the psbA mRNA.

• Journal of the Korean Society of Food Science and Nutrition
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• v.35 no.4
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• pp.470-475
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• 2006

In order to elucidate the differences of protein profiles among soybean cultivars, the protein composition of three conventional domestic soybean cultivars and two imported ones including glyphosate-tolerant HS2906 was analyzed by total nitrogen measurement, amino acid analysis and PAGE/densitometry. There were no statistically significant differences in the levels of any amino acid, including aromatic amino acids, between glyphosale-tolerant soybean and the conventional soybean WS82. In the extraction of protein, the SDS/buffer system was more efficient than the defatting/water system. The SDS-PAGE/densitometry analysis showed that there was a similar profile of proteins among cultivars, although the amount of total protein ranged from 380.2 mg/g to 423.9 mg/g. In addition, there was no discernable difference of protein profile between glyphosate- tolerant soybean (total protein amount, 380.2 mg/g) and the conventional soybean WS82 (390.2 mg/g), although the amount of ${\beta}$-conglycinin (55 kDa) was lower in glyphosate-tolerant soybean. Meanwhile, the amount of 25 kDa protein was greater in domestic soybean cultivars than imported ones. Thus, normal PAGE/ densitometry method would be useful to analyze the difference in protein profiles of soybean proteins, and furthermore Evaluate the protein profile of proteins between GMO and conventional soybean.

• Food Science of Animal Resources
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• v.25 no.3
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• pp.350-356
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• 2005

We examined the enhancement of thermotolerance for storage conferred on Lactobacillus acidophilus 30SC by adaptation to different stresses. The viable cells of Lactobacillus acidophilus 30SC were compared with their viability prior to heating at $45,\;55^{\circ}C\;and\;60^{\circ}C$. Heat-adapted ($45^{\circ}C$ for 15 min) L. acidophilus 30SC in MRS broth exhibited higher survivability at lethal temperature of $55^{\circ}C$ than control. Cellular protein profiles of L. acidophilus 30SC during heat adaptation were examined with SDS-PAGE, and scanning electron microscopy. When L. acidophilus 30SC was heat-adapted at $55^{\circ}C$ for 15min, 5 new protein spots of ca $8\~45\;kDa$ size were observed on 2D SDS-PAGE. It was presumed that new proteins of L. acidophilus 30SC were produced to adapt to the environment of higher growth temperature.

• Journal of Microbiology and Biotechnology
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• v.15 no.5
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• pp.1094-1099
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• 2005

Photosynthetic dinoflagellates contain a water-soluble, light-harvesting antenna called the peridinin-chlorophyll-protein (PCP) complex, which has an apoprotein with no sequence similarity to other known proteins. There are two forms of PCP apoproteins; the 15-kDa short form and the 32- to 35­kDa long form. The present study describes the PCP protein and its cDNA from Alexandrium tamarense. A cDNA library was constructed from mRNA isolated from A. tamarense. The complete PCP cDNA was generated by reverse-transcription coupled to polymerase chain reaction (RT-PCR), together with rapid-amplification of cDNA ends (RACE). The A. tamarense PCP cDNA encoded a 55-amino acid signal peptide and a 313-amino acid mature protein with a calculated mass of 32 kDa, which corresponded to that of the long form of PCP. Phylogenetic analysis indicated that the sequence of A. tamarense PCP did not cluster with the short-form PCPs, to which it was only about $55\%$ identical, but which were $79-83\%$ identical to other long-form PCPs. The deduced amino acid sequence of A. tamarense PCP contains an internal duplication, which suggests the possibility that long-form PCPs arose by gene duplication or by the fusion of genes encoding the short form. The abundance of PCP mRNA changed substantially in response to different light conditions, indicating the possible existence of a photo-acclimation response in A. tamarense.

• Animal cells and systems
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• v.1 no.1
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• pp.71-75
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• 1997

Male specific protein (MSP) was identified and purified from the hemolymph of Galleria melloneffa L. by electrophoresis and anion exchange chromatography. MSP has a native molecular weight of 55 kDa as determined by gel filtration chromatography and consists of a single unit with the apparent molecular weight of 27 kDa and has the pl of approximately 5.8. MSP is present in the hemolymph from day 8 pupae throughout the male adult. MSP was also found in pupal fat body, adult fat body, and adult testis.