• Title/Summary/Keyword: C-반응성 단백질

Search Result 357, Processing Time 0.024 seconds

Gelation Properties and Industrial Application of Functional Protein from Fish Muscle-1. Effect of pH on Chemical Bonds during Thermal Denaturation (기능성 어육단백질의 젤화 특성과 산업적 응용-1. 가열변성 중 화학결합에 미치는 pH의 영향)

  • Jung, Chun-Hee;Kim, Jin-Soo;Jin, Sang-Keun;Kim, Il-Suk;Jung, Kyoo-Jin;Choi, Yeung-Joon
    • Journal of the Korean Society of Food Science and Nutrition
    • /
    • v.33 no.10
    • /
    • pp.1668-1675
    • /
    • 2004
  • The effect of pH on surface hydrophobicity, sulfhydryl group, infrared spectrum, SDS-PAGE (sodium dodecyl sulfate-polyacrylamide gel electrophoresis) pattern and enthalpy was investigated in recovered protein from mackerel and frozen blackspotted croaker by alkaline processing. Hydrophobic residue in myofibrillar protein exposed to the surface of protein, and hydrophobic interaction were the highest around 6$0^{\circ}C$. The surface hydrophobicity was different between myofibrillar protein and myofibrillar protein including sarcoplasmic protein (recovered protein). The peak at 1636 c $m^{-l}$ was increased with pH, and the recovered protein was unfolded in alkali pH. Difference of surface and total sulfhydryl group at pH 7.0 and 10 was comparative high, and decrease of surface sulfhydryl group indicated formation of S-S bonds. Mackerel and frozen blackspotted croaker in alkaline pH showed bands of polymerized myosin heavy chain on SDS-PAGE pattern. The transition temperatures of recovered protein were 33.1, 44.3 and 65.5$^{\circ}C$. Gelation of recovered protein from alkali processing was estimated by increase of $\beta$-sheet structure by pH treatment, S-S bonds by oxidation of surface sulfhydryl group in heating, polymerization of myosin heavy chain in order.r.

Molecular Cloning of Novel Genes Specifically Expressed in Snailfish, Liparis tanakae (꼼치, Liparis tanakae에서 특이하게 발현되는 새로운 유전인자의 검색)

  • 송인선;이석근;손진기
    • Development and Reproduction
    • /
    • v.4 no.1
    • /
    • pp.67-77
    • /
    • 2000
  • Snailfish usually lives at the bottom of the sea and showed typical retrogressive change with specialized tissue structures of skin and skeletons. In order to obtain the specific genes of snailfish, highly expressed in the body, we made subtracted cDNA library and analyzed 200 clones. Totally 200 clones were obtained and sequenced, and among them 62 clones were turned out to be homologous to the known gene, i.e., thioesterase (9), myosin (8), creatine kinase (7), skeletal alpha-actin (6), parvalbumin b (5), ribosomal protein (5), type I collagen (3), muscle troponin (3), dopamine receptor (2), histatin (2), and heat shock protein (2), cystatin (1), lectin (1), statherin (1), secretory carrier membrane protein (1), keratin type I (1), desmin (1), chloroplast (1), muscle tropomyosin (1), reticulum calcium ATPase (1), ribonucleoprotein (1). The remaining 138 clones were low homologous or non-redundant genes through Genbank search. Especially 5 clones were novel and specifically expressed in the body tissues of Snailfish by in situ hybridization. Therefore, we analysed these 5 clones to identify the C-terminal protein structures and motifs, and partly defined the roles of these proteins in comparison with the expression patterns by in situ hybridization. C9O-77, about 5000 bp, was supposed to be a matrix protein expressed strongly positive in epithelium, myxoid tissue, fibrous tissue and collagenous tissue. C9O-116, about 1500 bp, was supposed to be a transmembrane protein which was weakly expressed in the fibrous tissue, epithelium tissue, and myxoid tissue, but strong in muscle tissue. C9O-130, about 1200 bp, was supposed to be an intracytoplasmic molecule usually in the epithelial cells. C9O-161, about 2000 bp, was weakly expressed in epithelium, muscle tissue and myxoid tissue, but specially strong in epithelium. C9O-171, about 1000 bp, was supposed to be a transcription factor containing zinc finger like domain, which was intensely expressed in the epithelium, muscle tissue, fibrous tissue, and in collagenous tissue.

  • PDF

Process Optimization of Meat Protein Hydrolysate of Ogae Wings by Response Surface Methodology and Its Characteristics Analysis (표면반응분석을 이용한 오계 날개육 단백질 가수분해 최적 생산 공정 개발과 생산물의 특성 분석)

  • Kim, A Yeon;Yoo, Sun Kyun
    • Journal of the Korean Applied Science and Technology
    • /
    • v.33 no.2
    • /
    • pp.293-303
    • /
    • 2016
  • Protein hydrolysate that shows physiological function such as antioxidant, suppression of hypertension, immunodulatory, alleviation of pain, and antimicrobial activity has been known as playing important role like hormone. This study was performed to optimize the hydrolysis of the wing's meat of Yosan-Ogae by a commercial protease. The ranges of processes were the reaction temperature of 40 to $60^{\circ}C$, pH 6 to 8, and enzyme concentration 1 to 3%(w/v). As a result, the optimization of process was determined at temperature of $48-50^{\circ}C$, pH of 7.0-7.2, and enzyme concentration of 3%(w/v), and degree of hydrolysis was 68 to 69% at above conditions. The molecular weight of hydrolysate was distributed to 500-1,200 Da and showed typical peptides. The amino acids of peptides showing presumably antioxidant activity such as histidine, proline, methionine, cystein, tyrosine, tryptophan, phenylalanine comprised about 43.07%. The glutamic acid was 13.6%. Therefore, we expect that those products are useful as functional food ingredients.

Process Optimization of Peptides Production from Protein of Sea Cucumber and Its Antioxidant Capacity Analysis (해삼 단백질로부터 펩타이드 제조 최적공정 확립 및 항산화 특성)

  • Ha, Yoo Jin;Yoo, Sun Kyun
    • Journal of the Korean Applied Science and Technology
    • /
    • v.34 no.2
    • /
    • pp.338-348
    • /
    • 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 performed to optimize the hydrolysis of protein of sea of cucumber by a flavourzyme. The ranges of processes were the reaction temperature of 40 to $60^{\circ}C$, pH 6 to 8, and enzyme concentration 0.5 to 1.5%(w/v). As a result, the optimization of process was determined at temperature of $48-50^{\circ}C$, pH of 7.0-7.2, and enzyme concentration of 1.0-1.1%(w/v), and degree of hydrolysis was 43-45 at above conditions. The molecular weight of hydrolysate was distributed to 500-3,500 Da and showed typical peptides. Inhibition concentration ($IC_{50}$) of peptides of DPPH radical scavenging activity, Superoxide anion radical scavenging activity, Hydroxy radical scavenging activity, $Fe^{2+}$ cheating activity was 1.25, 3.40, 10.3, and 22.11 mg/mL, respectively. Therefore, we expect that those products are useful as functional food ingredients.

Component proteins in crud extract of adult Paragonimus westermani purified by immunoaffinity chromatography using monoclonal antibodes (친화성크로마토그래피로 순수분리한 폐흡충 성충 성분단백질의 성상)

  • Kang, Shin-Yong;Kong, Yoon;Cho, Seung-Yull
    • Parasites, Hosts and Diseases
    • /
    • v.29 no.4
    • /
    • pp.363-370
    • /
    • 1991
  • 인체감염이 다발하는 폐흡충증의 혈청학적 진단에서 항원으로 사용하는 성충추출액은 여러단계의 질환 이행과정을 진단하는 항원으로서 문제가 있다. 이를 해결하려면 먼저 추출액내의 성분단백질의 성상을 파악할 필요가 있다. 이 연구에서는 폐흡충 성충 추출액으로 면역시킨 BALB/c mice의 비장세포와 SP2/0 형질세포종 세포를 세포융합하여 제작한 단세포군항체를 이용하여 친화성크로마토그래피로 폐흡충 성충의 구성단백질의 일부를 순수분리하고 성상을 관찰하였다. 그 결과는 다음과 같다. 1. 세포융합으로 PFCK-21, PFCK-44, PFCK-136, PFCK-189 등 4종류의 단세포군 항체를 얻었다. 그중 PFCK-21과 PFCK44는 17k Da, PFCK-136은 23, 46, 92 kDa 단백질에 반응하였고 PFCK-189는 여러종류의 단백질에 반응하였다. 2. PFCK-44 단세포군항체를 고리로 친화성 크로마토그래피를 실시하여 분리한 성분 단백질은 disc-PAGE상 4번째에 위치하고 분자량이 17 kDa로 알려진 단밸질이었다. 이 단밸질은 17 kDa의 monomer로 판단하였다. 면역조직화학염색을 실시한 결과 이 단밸질은 장관 상피세포에 반응하고 있었다. 3. PFCK-136 단세포군항체로 순수분리한 단밸질은 disc-PAGE상 1번 단밸질(440 kDa)이었으며 환원성 SDS-PAGE에서는 23 kDa 단밸질이었다. 면역조직화학염색으로 이 단세포군항체는 충란내 세포에 강하게 반응하고 있었다.

  • PDF

Involvement of Brca1 in DNA Interstrand Cross-link Repair Through Homologous Recombination-independent Process (재조합 비의존적 경로를 통한 DNA 사슬간 교차결합 복구에의 Brca1단백질의 기능)

  • Yun, Jean-Ho
    • Journal of Life Science
    • /
    • v.15 no.4 s.71
    • /
    • pp.542-547
    • /
    • 2005
  • Hypersensitivity of cells lacking Brcal to DNA interstrand .ross-link (ICL) agents such as cisplatin and mitomycin C(MMC) implicates the important role of Brcal in cellular response following ICL treatment. Brca1 plays an essential role in DNA double-strand break (DSB) repair through homologous recombination (HR)-dependent and -independent process. Recently, our group has been reported that Brca1 involves in cellular ICL response through HR-dependent repair process (Yun J. et at., Oncogene 2005). In this report, the involvement of Brca1 protein in HR-independent repair process is examined using isogenic $p53^{-/-}\;and\;p53^{-/-}\;Brcal^{-/-}$ mouse embryonic fibroblast (MEF) and psoralen cross-linked reporter reactivation assay. Brcal-deficient MEFs showed significantly low HR-independent repair activity compare to Brca1-proficient MEFs. Hypersensitivity to MMC and ICL reporter repair activity were restored by the reconstitution of Brca1 expression. Interestingly, MEFs expressing exon 11-deleted isoform of Brca1 $(Brca1^{\Delta11/\Delta11})$ showed high resistance to MMC and ICL reporter repair activity comparable to Brca1-reconstituted MEFs. Taken together, these results suggest that Brca1 involves in ICL repair through not only HR-dependent process but also HR-independent process using N-terminal RINC finger domain or C-terminal BRCT domain rather than exon 11 region which mediate interaction with Rad50.

Immunoelectrophoretic analysis of major component proteins In cystic fluid of Taenia solium metacestodes (면역전기영동법에 의한 유구낭미충 낭액의 구성 단백질 분석)

  • Yoon Kong;Seung-Yull Cho;Suk-Il Kim;Shin-Yong Kang
    • Parasites, Hosts and Diseases
    • /
    • v.30 no.3
    • /
    • pp.209-218
    • /
    • 1992
  • When cystic fluid of Taenia solium metacestodes (CF) was filtrated through Sephacryl S-300 Superfine, major proteins were in fractions III add IV Major protein in fraction III was Band C protein of 150 kDa and that in fraction IV was Band N protein (Choi et of., 1990). When CF was electrophoresed in 0.9% agarose gel and reacted with anti-CF rabbit serum (RACF), two main bands, a long outer and a short inner band, were precipitated, together with 8 minor bands. RACF reacted with fraction III forming the long outer band whereas RACF formed the short infer band with fraction IV in immunoelectrophoresis (IEP) The long outer precipitin band of CF fraction III was similar to antigen B in hydatid fluid (HF) of Oriol et at. (1971), while the short inner band of CF fraction IV was similar to HF antigen 5 of Caption et at. (1967) . When HF was reacted with RACF, the short inner band was immunoprecipitated without forming the long outer band. Common antigenicity between CF and HF seemed to exist in fraction IV rather than in fraction III of CF. Patient sera of neurocysticercosis reacted more frequently with fraction III than with fraction IV.

  • PDF

Cloning of cDNA Encoding Putative Cellular Receptor Interacting with E2 protein of Hepatitis C Virus (C형 간염바이러스 E2 단백질에 결합하는 추정 세포수용체 cDNA의 클로닝)

  • 이성락;백재은;석대현;박세광;최인학
    • Journal of Life Science
    • /
    • v.13 no.4
    • /
    • pp.541-550
    • /
    • 2003
  • E2 glycoprotein of hepatitis C virus (HCV) comprises a surface of viral particle together with E1 glycoprotein, and is thought to be involved in the attachment of HCV viral particle to receptor (s) on the permissible cells including hepatocytes, B cells, T cells, and monocytes. We constructed a phage library expressing cellular proteins of hepatocytes on the phage surface, which turned out to be 8.8${\times}$$10^5$ cfu of diversity and carried inserts in 95% of library. We screened both cDNA phage library and 12-mer peptide library to identify the cellular proteins binding to E2 protein. Some intracellular proteins including tensin and membrane band 4.1 which are involved in signal transduction of survival and cytoskeleton organization, were selected from cDNA phage library through several rounds of panning and screening. On the contrary, membrane proteins such as CCR7, CKR-L2, and insulin-like growth factor-1 receptor were identified through screening of peptide library. Phages expressing peptides corresponding to those membrane proteins were bound to E2 protein specifically as determined by neutralization of binding assay. Since it is well known that HCV can infect T cells as well as hepatocytes, we examined to see if E2 protein can bind to CCR7, a member of C-protein coupled receptor family expressed on T cells, using CCR7 transfected tells. Human CCR7 cDNA was cloned into pcDNA3.1(-) vector and transfected into human embryonic kidney cell, 293T, and expressed on the surface of the cell as shown by flow cytometer. Binding assay of E2 protein using CCR7 transfected cells indicated that E2 protein bound to CCR7 by dose-dependent mode, giving rise to the possibility that CCR7 might be a putative cellular receptor for HCV.

An Enzyme-Linked Immunosorbent Assay for Detection of Cooked Goat Meat (가열 염소육의 판별을 위한 효소면역측정법)

  • Kim, Hyun-Jung;Shon, Dong-Hwa
    • Korean Journal of Food Science and Technology
    • /
    • v.32 no.3
    • /
    • pp.538-543
    • /
    • 2000
  • This study was conducted to develop an enzyme-linked immunosorbent assay(ELISA) for the determination of cooked goat meat. Muscle proteins were extracted from goat meat by heating at $98^{\circ}C$ for 15 min. Major thermostable(TS) protein, whose size and pI are 36 and 38 kDa and 4.5 respectively, were purified by DEAE-Sephadex A-50 and Sephadex G-75 column chromatography. The TS protein was immunized into rabbits in order to produce goat specific antibodies. Competitive indirect ELISA(ciELISA) was established by using the anti-TS antibody. The antibody showed high reactivity toward the TS antigen and the boiled goat meat extract but it did not show any reactivities toward extracts of boiled chicken, pork, lamb, and beef. Thus, this ciELISA developed in this study could be applicable to identify goat species from cooked meat.

  • PDF