• Journal of environmental and Sanitary engineering
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• v.12 no.2
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• pp.59-64
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• 1997

For purification of a 70kDa toxic protein of mosquitocidal delta-endotoxin from B. thuringiensis strain H9B, immuno-affinity chromatography was performed. After separation of 70kDa toxic proteins from the delta-endotoxin of the strain H9B on SDS-PAGE, the 70kDa toxic protein was subcutaneously injected into rabbit for making a polyclonal antibody. A anti-70kDa toxic protein was purified by a column chromatography packed with protein A-sepharose 4B gels. The 70kDa toxic protein from delta-endotoxin of the strain H9B was also purified by an immuno-affinity chromatography packed with CNBr-activated sepharose 4B gels conjugated anti-70kDa toxic protein after elution with 1/10M citric acid-1/5M Na$_{2}$HPO$_{4}$ buffer(pH3.2) containing 0.5M NaCl. The 70kDa toxic protein was purified through only one step-separation system, was demonstrated by SDS-PAGE and immunoblot.

• The Korean Journal of Zoology
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• v.35 no.2
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• pp.203-210
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• 1992

Hsp70, a 70 kDa protein, is the maior protein expressed when cells are heat-shocked. A cDNA library from mouse ID13 cells was screened with the human hsp70 gene as a probe, and a positive clone was obtained. The positive clone was subcloned into puc19 and the precise restriction was obtained. The CDNA was sequenced by the Sanger's dideoxv termination method. Single open reading frame that codes for a protein of 70 kDa was found. The DNA sequence of the cloned mouse DNA shows great homology (66-90%) with other mouse hsp70 genes and somewhat less homology (50",) with E. coli hsp70 gene (dnak). With the exception of one amino acid, the protein sequence deduced from the CDNA is identical to the mouse that shock cognate protein 70 (hsc70) that is constitutivelv expressed at normal temperature. The result suggests that the cloned CDNA encodes a hsc70 family rather than a heatinducible family.mily.

• Journal of Photoscience
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• v.7 no.3
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• pp.123-128
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• 2000

Phosphorylation of cellular proteins is a key regulatory mehanism for signal transduction pathway in living cells. Phytochrome, a red/far-red light photoreceptor in plants, is known to employ protein phosphorylation for its light signaling, although its detauked mechanism is still ambiguous. This study is intended to identify the phosphoproteins and protein kinases that are regulated by phytochrome, by employing transgenic rice seedlings that overexpress Arabidopsis phytochrome A. Red light stimulated phsophorylation of a 70 kDa protein and far-red light negated the effect. The red light induced phosphotylation of the 70 kDa protein was strongly activated by heparin and inhibited by poly-L-lysine, suggesting that the 70 kDa protein phosphorylating kinase belongs to GSK-3/SHAGGY protein kinase that has functional roles in establishing cell fate and pattern formation in Drosophila. Taken together with the fact that phytochrome controls plant development, these results may suggest that a GSK-3/SHAGGY-related protein kinase in plant(ASK) is likely to be involved in phytochrome signal transduction.

• Journal of Microbiology and Biotechnology
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• v.14 no.4
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• pp.772-776
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• 2004

Physiological and molecular characteristics of Bacillus thuringiensis SR6 and SR8 were investigated, and phase contrast and electron microscopies revealed that a large rhomboidal crystal protein was present in the sporulating cells. SDS-PAGE and Western blot analyses showed that B. thuringiensis SR8 produced 70 kDa protein much more than other proteins, and that the 70 kDa protein could bind to the antibody of B. thuringiensis subsp. tenebrionis-crystal toxin protein, indicating that the crystal 70 kDa protein has an immunological homology with B. thuringiensis subsp. tenebrionis-crystal toxin protein. The DNA fragment of B. thuringiensis subsp. tenebrionis-toxin gene was detected in B. thuringiensis SR6 and SR8 by using PCR amplification analysis. Furthermore, the insect bioassay showed the insecticidal activity against Colorado potato beetle larvae. Based on the physiological and molecular similarities to B. thuringiensis subsp. tenebrionis, it is suggested that the B. thuringiensis SR6 and SR8 may be mutants of the B. thuringiensis subsp. tenebrionis strain overexpressing the crystal of 70 kDa toxin protein.

• Journal of fish pathology
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• v.28 no.3
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• pp.133-143
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• 2015

The antigenic proteins of Lymphocystis disease virus (LCDV) from tumors of olive flounder, Paralichthys olivaceus, are described following characterization by mass spectrometry. In SDS-PAGE, predominant protein bands were observed at 114, 88, 70, 54, 52, 47, 42 and 24 kDa. Western blot analysis showed that antisera reacted strongly at molecular weights of 114, 67 and 54 kDa, and reacted weakly at molecular weights of 74, 70, 36, 24 and 22 kDa. In the identification of LCDV antigenic proteins by matrix-assisted laser desorption ionization (MALDI) TOF mass spectrometry, 10 of 14 excised bands consisted mostly of proteins with amino acid sequences that matched LCDV-C (lymphocystis disease virus isolate China) ORFs. Strong antigens with molecular weights of 114, 67 and 54 kDa were identified as LDVICp236 (chromosome segregation ATPase), LDVICp033 (membrane bound metallopeptidase) and LDVICp157 (hypothetical protein), respectively. Minor antigens with molecular weights of 70, 36, 24 and 22 kDa proteins were identified as LDVICp160 (acetyl-coA hydrolase), LDVICp213 (hypothetical protein), LDVICp039 (hypothetical protein) and LDVICp213 (hypothetical protein). However, the major capsid protein (LDVICp043) did not react with the polyclonal antibody.

• Korean Journal of Microbiology
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• v.33 no.4
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• pp.242-246
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• 1997

The protein profile of Synechococcus sp. cyanophage was investigated employing SDS-PAGE. The phage appears to be composed of two major proteins of 97 and 52 kDa and at least seven minor proteins of 70, 65, 60, 40, 35, 28, and 6 kDa. It seems that each subunit is combined to form a multimer although any disulfide bond does not exist in the phage structure. Lytic activity of the phage particle against cell wall was detected around the 52 kDa on renaturing SDS-PAGE using heat-killed Micrococcus luteus cells as substrate. The activity has the optimal pH between 9 and 10, and slightly inhibited by EDTA.

• Preventive Nutrition and Food Science
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• v.13 no.3
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• pp.204-211
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• 2008

Fish protein hydrolysates (FPHs) with different degrees of hydrolysis by treatment with alcalase, pronase, flavourzyme and trypsin and isolated peptide were prepared from Hwangtae (yellow dried pollack, Theragra chalcogramma). Hwangtae protein hydrolysate was fractionated according to the molecular weight into six major types of APO1 (1.3 kDa), APO2 (1 kDa), APO3 (<1 kDa), APACE (<1 kDa), APG1 (70 kDa) and APG2 (70 kDa) isolated from the hydrolysate using consecutive chromatographic methods. Soluble peptide were produced from Hwangtae and evaluated for their nutritional and functional properties. Some functional properties of FPHs were assessed and compared with those of egg albumin or the soybean protein. APO2 had the highest nitrogen solubility value (94.2%), emulsion capacity and emulsion stability of the Alaska Pollack peptide ranged from 12.4 to 39.5 (mL of oil per 200 mg of protein) and 44.0% to 77.5%, respectively. Highest and lowest fat adsorption values were observed for APG1 (9.9 mL of oil per gram of protein) and APO3 (3.8 mL of oil per gram of protein), respectively.

• Journal of the Korean Magnetic Resonance Society
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• v.20 no.4
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• pp.138-142
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• 2016

Replication Protein A (RPA) is the eukaryotic single-stranded DNA binding protein. It involves in DNA replication, repair, and damage response. Among three subunits, RPA70 has a protein-protein binding domain (RPA70N) at the N-terminal. It has known that the domain recruits several damage response proteins to the damaged site. Also, it is suggested that there are more candidates that interact with RPA70N. Even though several studies performed on the structural aspects of RPA70N and its ligand binding, the backbone assignments of RPA70N is not available in public. In this study, we present the backbone assignments of RPA70N.

• Journal of the Korean Applied Science and Technology
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• v.34 no.3
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• pp.673-682
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• 2017

Protein hydrolysates derived from plants and animals having antioxidant, suppression of hypertension, immunodulatory, alleviation of pain, and antimicrobial activity has been known as playing important role like hormone. This study was fractioned to hydrolysis of Ogae egg white protein using the ultrafiltration. The antioxidant activity of the produced peptides was analyzed. As a result, the maximum value of DPPH radical scavenging was 1 kDa(70.83 %), hydroxy radical scavenging was 5 kDa(47.01 %), superoxide anion radical scavenging was 5 kDa(40.57 %), and $Fe^{2+}$ chelation ability was 5 kDa(29.87 %). Furthermore, the antioxidant Inhibition concentration ($IC_{50}$) of peptides was evaluated for each fraction. As a result, the maximum value of HDS was superoxide anion radical scavenging($IC_{50}$, 5.42 mg/ml). 1 kDa was $Fe^{2+}$ chelation ability($IC_{50}$, 1.67 mg/ml), 5 kDa was $Fe^{2+}$ cheating ability($IC_{50}$, 2.09 mg/ml), 10 kDa was $Fe^{2+}$ cheating ability($IC_{50}$, 2.61 mg/ml), papain was $Fe^{2+}$ cheating ability($IC_{50}$, 4.53 mg/ml). Therefore, we expect that peptides produced from Ogae egg white protein using 5 kDa fraction are useful as an antioxidant functional food ingredients.

• Preventive Nutrition and Food Science
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• v.19 no.4
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• pp.327-332
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• 2014

The purpose of the current study was to determine the effects of the introduction of polysaccharide chains onto the molecular surface of buckwheat proteins on buckwheat protein surface functionality. The whole buckwheat protein fraction (WBP) was prepared using 50 mM phosphate buffer (pH 7.5) containing 0.5 M NaCl and covalently linked with 6 kDa, 17.5 kDa, 40 kDa, 70 kDa, or 200 kDa dextran by Maillard-type glycation through controlled dry-heating at $60^{\circ}C$ and 79% relative humidity for two weeks. Conjugation with 40 kDa dextran improved the water solubility and emulsifying properties of WBP without causing a serious loss of available lysine; 84.9% of the free amino groups were conserved. In addition, we found that the introduction of dextran chains onto the molecular surfaces of WBP attenuated the antigenicity of WBP.