• 제목/요약/키워드: Soluble Protein

검색결과 1,476건 처리시간 0.027초

황해산 두족류의 가용성 단백질에 대한 연구(II) (Soluble Proteins Analysis of Class Cephalopoda in the Yellow Sea(II))

  • 허회권;황규린
    • 한국양식학회지
    • /
    • 제10권4호
    • /
    • pp.425-433
    • /
    • 1997
  • 황해산 두족류 6종(참갑오징어, Sepia esculenta ; 쇠갑오징어, Sepiella japonica : 한치꼴뚜기, Loligo chinensis : 살오징어, Todarodes pacificus : 참꼴뚜기, Loligo beka : 낙지, Octopus minor)의 안구단백질을 추출하여 항원-항체 교차반응을 실시하였다. 쇠갑오징어, 살오징어와 낙지의 안구단백질로 항혈청(antiserum)을 제작하였으며 갑오징어목, 살오징어목 및 낙지목에 속하는 두족류 6종의 안구단백질을 항원(antigen)으로 사용하였다. 갑오징어목 속하는 쇠갑오징어 및 참갑오징어에서 항원-항체 반응 양상이 매우 뚜렷하였으며 종간 비교에 기준이 될 수 있고 또한 유의성있는 침강선을 볼 수 있었다. 또한 gel filtration chromatography 방법으로 살오징어의 안구단백질을 분획하여 crystallin을 분리하였으며, 주 분획을 SDS-PAGE 전기영동 방법으로 분자량을 추정해 본 결과 약 20-35 KDa 였다.

  • PDF

Post-Infectional Biochemical Changes in Mulberry Due to Xanthomonas campestris pv. mori Induced Bacterial Leaf Spot

  • Maji, M.D.;Sengupta, T.;Das, C.;Urs, S.Raje
    • International Journal of Industrial Entomology and Biomaterials
    • /
    • 제9권2호
    • /
    • pp.255-259
    • /
    • 2004
  • Post-infectional biochemical changes due to Xanthomonas campestris pv. mori (Xcm) infection in five elite mulberry varieties viz., $S_1$, $S_{1635}$, $V_1$, RF $S_{175}$ and JRH was studied under inoculated condition. It was revealed that total soluble sugar and protein content was significantly declined in all the varieties due to X. campestris infection. Total phenol content was at par prior to inoculation in all varieties, but it was significantly increased in $S_1$, RF $S_{175}$, $S_{1635}$ and JRH 7 days after inoculation. The correlation coefficient (r) between total soluble sugar and total phenol content was found positive (r = 0.825) and statistically significant. Similarly, correlation coefficient (r) between total soluble protein and phenol content was found positive (r = 0.897) and statistically significant. The present study indicates that X. campestris infected leaves are nutritionally inferior in quality and the duration of phenol production in a mulberry variety play decisive role on disease resistance.nce.

전복 Paramyosin의 분리 및 그 성질 (PARAMYOSIN OF THE ABALONE, NOTOHALIOTIS DISCUS)

  • 변재형
    • 한국수산과학회지
    • /
    • 제5권1호
    • /
    • pp.29-38
    • /
    • 1972
  • 복족류 근육단백질을 다른 연분동물의 그것과 비교생화학적으로 검토하고져 전복을 선정하여 근육단백질의 조성을 측정하고 그 주요 구성단백질인 paramyosin을 정열 단리하여 몇가지 생물물리화학적인 성질에 관하여 실험하였다. 전복근육의 단백조성은 수용성구분 $19\~22\%$, 염용성구분 $27\~39\%$, 알카리 가용성구분 $20\~26\%$, 그리고 stroma $20\~28\%$이었다. 염용성구분은 초원심분석에서 Paramyosin이 약 $65\%$, actomyosin이 약 $30\%$, myosin이 약$5\%$로서 이루어져 있음을 알았다. 그리고 초원심분석상 균질의 단일 표품으로 판명 분리된 본 실험에서의 전복 Paramyosin은 침항정수($S^{\circ}\;_{20,\;{\omega}$) 3.14s, 정전염용 $0.35{\mu}$ 이상, $25^{\circ}C$에서의 고유점도는 3.1이었고, 한편 동 Paramyosin은 염석분석에서 이 단백질의 염석절위가 $18\~30\%$이었다. 그리고 아미노산 분석결과, 구성아미노산은 arginine, aspartic acid, glutamic acid등이 많이 함유되어 있고, proline과 tryptophane이 흠여되어 있는 점 등 2매패류의 아미노산조성과 비슷하였으나, Iysine/arginine의 비는 0.61로서 2매패류보다 낮았다.

  • PDF

Production of the taste-modifying protein, miraculin, in transgenic lettuce

  • Ezura, Hiroshi;Sun, Heyon-Jin
    • 한국식물생명공학회:학술대회논문집
    • /
    • 한국식물생명공학회 2005년도 추계학술대회 및 한일 식물생명공학 심포지엄
    • /
    • pp.126-131
    • /
    • 2005
  • Richadella dulcifica, a native shrub in tropical West Africa, gives red berries that have the unusual property of modifying a sour taste into a sweet taste. The red berries contain a taste-modifying protein named miraculin. A synthetic gene encoding miraculin was placed under the control of constitutive promoters and transferred to lettuce. High expression of miraculin was obtained, with accumulation of up to 1% total soluble protein in lettuce leaf. In addition, the miraculin expressed in lettuce possesses a taste-modifying activity.

  • PDF

"OPEN" STRUCTURE OF SecA PROTEIN OF ESCHERICHIA COLI IN SOLUTION

  • Maengseok Song;Kim, Hyounman
    • 한국생물물리학회:학술대회논문집
    • /
    • 한국생물물리학회 1996년도 정기총회 및 학술발표회
    • /
    • pp.27-27
    • /
    • 1996
  • SecA protein which has a pivotal role in the preprotein cranslocation across the inner membrane of Escherichia coli is a water-soluble protein with an unusual property of penetrating the membrane readily. An interesting and important question is what structural characteristics of SecA enables its ready penetration of lipid bilayer. The conformational properties of SecA in solution at 3$0^{\circ}C$, pH 7.5 were observed by hydrogen-tritium (HT) exchange, and denaturant-induced denaturation/renaturation and thermal unfolding. (omitted)

  • PDF

High-Level Production of Spider Silk Protein by Fed-Batch Cultivation of Recombinant Escherichia coli and Its Purification

  • 이석재;이상엽
    • 한국생물공학회:학술대회논문집
    • /
    • 한국생물공학회 2001년도 추계학술발표대회
    • /
    • pp.719-722
    • /
    • 2001
  • Silk proteins from Nephila clavipes are fibrous proteins containing repetitive sequences with both crystalline and amorphous domains. In order to obtain high-level production of silk protein, the synthetic genes had 16 contiguous units of the consensus repeat sequence of the silk protein were expressed in Escherichia coli BL21(DE3) under the strong inducible T7 promoter. For production of recombinant silk protein in large amounts, pH-stat fed-batch cultures were carried out. The recombinant silk protein was produced as soluble forms in E. coli, and the recombinant silk protein content was as high as 11% of the total protein. When cells were induced at $OD_{600}$ of 60, the amount of silk protein produced was 6.49 g/L. After simple purification steps, 9.2 mg of silk protein that was more than 80% pure was obtained from a 50 mL culture, and the recovery yield was 26.3%.

  • PDF

Structural characterization of calmodulin like domain of ryanodine receptor type 1

  • Song, Yonghyun;Kang, Sunmi;Park, Sunghyouk
    • 한국자기공명학회논문지
    • /
    • 제19권2호
    • /
    • pp.74-82
    • /
    • 2015
  • Ryanodine receptor (RyR) is one of the two major $Ca^{2+}$ channels in membranes of intracellular $Ca^{2+}$ stores and is found in sarcoplasmic reticulum (SR), endoplasmic reticulum (ER). RyR1 is also the major calmodulin-binding protein of sarcoplasmic reticulum membranes. Residues 4064-4210 in the RyR1 polypeptide chain has similar primary sequence with calmodulin (CaM) and was designated as CaM-like domain (CaMLD). When expressed as a recombinant peptide, CaMLD showed several CaM-like properties in previous studies. Still, previous studies of CaMLD were focused on protein-protein interactions rather than its own properties. Here, we studied the expression of CaMLD and its sub-domains corresponding to each lobe of CaM in Escherichia coli. CaMLD could be obtained only as inclusion body, and it was refolded using urea solubilization followed by dialysis. Using spectroscopic approaches, such as NMR, circular dichroism, and gel filtration experiment, we found that the refolded CaMLD exists as nonspecific aggregate, even though it has alpha helical secondary structure. In comparison, the first half of CaMLD (R4061-4141) could be obtained as natively soluble protein with thioredoxin fusion. After the removal of the fusion tag, it exhibited folded and helical properties as shown by NMR and circular dichroism experiments. Its oligomeric status was different from CaMLD, existing as dimeric form in solution. However, the second half of the protein could not be obtained as soluble protein regardless of fusion tag. Based on these results, we believe that CaMLD, although similar to CaM in sequence, has quite different physicochemical properties and that the second half of the protein renders it the aggregative properties.

갑오징어(Sepia esculenta)갑 칼슘으로 회수한 surimi 가공폐수 단백질의 어묵소재로서 이용 (Utilization of a Soluble Protein Recovered from Surimi Wastewater by Calcium Powder of Cuttle, Sepia esculents Bone)

  • 김진수;조문래;허민수
    • 한국수산과학회지
    • /
    • 제36권3호
    • /
    • pp.204-209
    • /
    • 2003
  • Utilization of soluble protein recovered from surimi wastewater using calcium powder of cuttle bone were examined. The crude ash content of the heat-induced surimi gel was increased linearly by increasing substitution ratio of recovered protein-ATC toward commercial surimi. Moisture (approximately $76\%$) and lipid $(0.2\%)$ contents were not change, but their protein contents were decreased 15.7 to $14.3\%$ depend on increasing of substitution ratio. The white index of the heat-induced surimi gel by color meter was increased up to $10\%$ of substitution ratio. There were no difference between $0\%\;and\;5\%$ substituted surimi gel in the gel strength. The sensory score on white index and texture of the heat-induced surimi gel did not change in 0 to $10\%$ as a substitution ratio of recovered protein-ATC toward commercial surimi, while decreased in more $15\%.$ The optimal substitution ratio of recovered protein-ATC as a bulking agent was $10\%.$ The heat-induced surimi gel prepared with $10\%$ substitution of recovered protein-ATC was similar to the content and composition of total amino. acids, and superior to calcium content and the ratio of calcium and phosphorus toward those of commercial surimi.

New Protein Extraction/Solubilization Protocol for Gel-based Proteomics of Rat (Female) Whole Brain and Brain Regions

  • Hirano, Misato;Rakwal, Randeep;Shibato, Junko;Agrawal, Ganesh Kumar;Jwa, Nam-Soo;Iwahashi, Hitoshi;Masuo, Yoshinori
    • Molecules and Cells
    • /
    • 제22권1호
    • /
    • pp.119-125
    • /
    • 2006
  • The rat is an accepted model for studying human psychiatric/neurological disorders. We provide a protocol for total soluble protein extraction using trichloroacetic acid/acetone (TCA/A) from rat (female) whole brain, 10 brain regions and the pituitary gland, and show that two-dimensional gel electrophoresis (2-DGE) using precast immobilized pH (4-7) gradient (IPG) strip gels (13 cm) in the first dimension yields clean silver nitrate stained protein profiles. Though TCA/A precipitation may not be "ideal", the important choice here is the selection of an appropriate lysis buffer (LB) for solubilizing precipitated proteins. Our results reveal enrichment of protein spots by use of individual brain regions rather than whole brain, as well as the presence of differentially expressed spots in their proteomes. Thus individual brain regions provide improved protein coverage and are better suited for differential protein detection. Moreover, using a phosphoprotein-specific dye, ingel detection of phosphoproteins was demonstrated. Representative high-resolution silver nitrate stained proteome profiles of rat whole brain total soluble protein are presented. Shortcomings apart (failure to separate membrane proteins), gel-based proteomics remains a viable option, and 2-DGE is the method of choice for generating high-resolution proteome maps of rat brain and brain regions.

Expression of Escherichia coli Heat-labile Enterotoxin B Subunit (LTB) in Saccharomyces cerevisiae

  • Rezaee Mohammad Ahangarzadeh;Rezaee Abbas;Moazzeni Seyed Mohammad;Salmanian Ali Hatef;Yasuda Yoko;Tochikubo Kunio;Pirayeh Shahin Najar;Arzanlou Mohsen
    • Journal of Microbiology
    • /
    • 제43권4호
    • /
    • pp.354-360
    • /
    • 2005
  • Heat-labile enterotoxin B subunit (LTB) of enterotoxigenic Escherichia coli (ETEC) is both a strong mucosal adjuvant and immunogen. It is a subunit vaccine candidate to be used against ETEC-induced diarrhea. It has already been expressed in several bacterial and plant systems. In order to construct yeast expressing vector for the LTB protein, the eltB gene encoding LTB was amplified from a human origin enterotoxigenic E. coli DNA by PCR. The expression plasmid pLTB83 was constructed by inserting the eltB gene into the pYES2 shuttle vector immediately downstream of the GAL1 promoter. The recombinant vector was transformed into S. cerevisiae and was then induced by galactose. The LTB protein was detected in the total soluble protein of the yeast by SDS-PAGE analysis. Quantitative ELISA showed that the maximum amount of LTB protein expressed in the yeast was approximately $1.9\%$ of the total soluble protein. Immunoblotting analysis showed the yeast-derived LTB protein was antigenically indistinguishable from bacterial LTB protein. Since the whole-recombinant yeast has been introduced as a new vaccine formulation the expression of LTB in S. cerevisiae can offer an inexpensive yet effective strategy to protect against ETEC, especially in developing countries where it is needed most.