• Title/Summary/Keyword: Protein S

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Identification of Highly Transcribed Genes in Japanese Oak Silkworm, Antheraea yamamai, Using PCR-Based cDNA Library

  • Lee, Jin-Sung;Kim, Ki-Hwan;Goo, Tae-Won;Yun, Eun-Young;Kang, Seok-Woo;Suh, Dongs-Sang;Hwang, Jae-Sam
    • International Journal of Industrial Entomology and Biomaterials
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    • 제1권2호
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    • pp.171-175
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    • 2000
  • Determined sequences of 384 randomly selected clones in a PCR-based cDNA library of Antheraea yamamai could identify expressed sequence tags (ESTs) of highly expressed gene. One EST (fibroin) appeared 15 times, one EST (40S ribosomal protein S18) twelve times, one EST (ribosomal protein S24a) eleven times, ten times (ribosomal protein S8), nine times (60S ribosomal protein L10A), seven times (60S ribosomal protein S15A, S17, S17 and seroin), six times (ribosomal protein S8), five times (ribosomal protein S24, mariner transposase and P8 protein), four times (serpin 2), three times (heat shock protein 70 and poly A binding protein), and the remaining 6 ESTs twice (amylase, KIAA1006, elongation factor-1, transposon mag, translation initiation factor 4C, QM protein, transposase). Therefore, the 94 EST make it possible to identify 24 redundant clones that are candidates for highly expressed genes in posterior silk gland of this insect. The 24 redundant EST clones were identified in GenBank, but none of them was related to A. yamamai, suggesting that there are many unidentified genes which are highly expressed in the A. yamamai genome.

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콩 품종의 단백질함량과 아미노산 조성 (Protein and Content Amino Add Composition of Soybean Cultivars)

  • 홍은희;김석동;김용호;정길웅
    • 한국작물학회지
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    • 제35권5호
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    • pp.403-412
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    • 1990
  • 단백질 및 지방질의 주요한 공급원인 콩은 오래전부터 다양한 용도로 우리의 식생활에 이용되어 왔으며 앞으로도 안정적인 단백질 공급원을 위해서는 양질 고단백 콩 신품종 육성에 많은 노력을 기울여야 한다. 따라서 콩 단백질의 특성에 관한 연구내용들을 정리한 바 다음과 같이 요약할 수 있었다.1. 콩 종실 부위중 배아와 자엽은 전체 콩 종실무게의 2.4%와 90.3%를 차지하며 단백질도 건물중으로 40%이상 함유되어 있는 영양적으로 중요한 부분이 된다. 2. 콩 종실 단백질의 대부분은 Globulin이 차지한다. 3. 콩 종실 단백질의 Amino산 조성은 Glutamic acid, Aspartic acid, Arginin의 순으로 다량 함유되어 있으며 Cystine, Methionine, Thyrosine이 적게 함유되어 있다. 4. 콩 종실의 주요 단백질 분획은 7S와 11S로 되어 있으며 11S가 7S보다 함류황 Amino산 함유량이 많다. 5. 콩의 가용성 단백질 함량이 높을수록 두부의 수율도 증가했으며 이들의 상관계수는 0.96을 보였다.

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분리대두단백질 종류에 따른 증편의 품질특성 (A study on the Quality Properties of Jeung-pyun added SPI(Soybean protein isolate))

  • 홍금주;김명희;김강성
    • 한국식품조리과학회지
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    • 제23권6호
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    • pp.810-817
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    • 2007
  • The quality properties of Jeung-pyun made with soybean protein isolate(SPI) were investigated. The SPI Jeung-pyun was manufactured using 3% whole protein, 7S protein or 11S protein(w/w). The redness values (a-values) of the Jeung-pyun were negative and the yellowness(b-value) of the control group was significantly lower compared to the other samples. The textural characteristics of the Jeung-pyun were influenced by the additions of SPI. The Jeung-pyuns containing soybean flour, whole protein, 7S and 11S protein had increases in springiness, but decreases in cohesiveness. In the sensory evaluation, overall desirability, sweetness, and moistness were highest in the whole protein group. The control group showed the highest scores for hardness and toughness, and the scores for after-taste and adhesiveness were the highest in the samples made with soybean flour. The 7S and 11S additions showed high scores in terms of color and springiness. In the analyses for consumer acceptance and sensory quality intensity, the whole protein addition had significantly higher scores for general acceptability and the Makgeolli flavor. Hardness was highest for the control group and the Makgeolli flavor was strongest with the soybean flour addition.

인체 S100A6 단백질에 특이한 단일클론 항체 (Characterization of the Monoclonal Antibody Specific to Human S100A6 Protein)

  • 김재화;윤선영;주종혁;강호범;이영희;최용경;최인성
    • IMMUNE NETWORK
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    • 제2권3호
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    • pp.175-181
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    • 2002
  • Background: S100A6 is a calcium-binding protein overexpressed in several tumor cell lines including melanoma with high metastatic activity and involved in various cellular processes such as cell division and differentiation. To detect S100A6 protein in patient' samples (ex, blood or tissue), it is essential to produce a monoclonal antibody specific to the protein. Methods: First, cDNA coding for ORF region of human S100A6 gene was amplified and cloned into the expression vector for GST fusion protein. We have produced recombinant S100A6 protein and subsequently, monoclonal antibodies to the protein. The specificity of anti-S100A6 monoclonal antibody was confirmed using recombinant S100A recombinant proteins of other S100A family (GST-S100A1, GST-S100A2 and GST-S100A4) and the cell lysates of several human cell lines. Also, to identify the specific recognition site of the monoclonal antibody, we have performed the immunoblot analysis with serially deleted S100A6 recombinant proteins. Results: GST-S100A6 recombinant protein was induced and purified. And then S100A6 protein excluding GST protein was obtained and monoclonal antibody to the protein was produced. Monoclonal antibody (K02C12-1; patent number, 330311) has no cross-reaction to several other S100 family proteins. It appears that anti-S100A6 monoclonal antibody reacts with the region containing the amino acid sequence from 46 to 61 of S100A6 protein. Conclusion: These data suggest that anti-S100A6 monoclonal antibody produced can be very useful in development of diagnostic system for S100A6 protein.

MUSCLE PROTEIN SYNTHESIS IN VITRO IN CHICKS FED A LOW-PROTEIN DIET

  • Kita, K.;Kuzuya, Y.;Matsunami, S.;Okumura, J.
    • Asian-Australasian Journal of Animal Sciences
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    • 제9권2호
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    • pp.171-174
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    • 1996
  • Muscle protein synthesis in vitro was measured in chicks fed low-protein(10% CP) and control(20% CP) diets. Right leg muscles (M. gastrocnemius) were mounted on a support made of stainless steel to stretch in constant tension, whereas left leg muscles were unmounted. Both leg muscles were incubated in Dulbecco's modified Eagle's medium including L-[$4-^3H$] phenylalanine for 60 min to measure in vitro protein synthesis. There was no significant difference in fractional synthesis rate(FSR) of muscle protein between both dietary protein levels, whereas FSR with stretch in constant tension was significantly higher than that without constant tension due to an increase in the absolute synthesis rate(ASR) per unit RNA(the efficiency of RNA to synthesize protein). The ASR of muscle protein in chicks fed the control diet was significantly higher than that in the low-protein diet group.

Computational approaches for molecular characterization and structure-based functional elucidation of a hypothetical protein from Mycobacterium tuberculosis

  • Abu Saim Mohammad, Saikat
    • Genomics & Informatics
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    • 제21권2호
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    • pp.25.1-25.12
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    • 2023
  • Adaptation of infections and hosts has resulted in several metabolic mechanisms adopted by intracellular pathogens to combat the defense responses and the lack of fuel during infection. Human tuberculosis caused by Mycobacterium tuberculosis (MTB) is the world's first cause of mortality tied to a single disease. This study aims to characterize and anticipate potential antigen characteristics for promising vaccine candidates for the hypothetical protein of MTB through computational strategies. The protein is associated with the catalyzation of dithiol oxidation and/or disulfide reduction because of the protein's anticipated disulfide oxidoreductase properties. This investigation analyzed the protein's physicochemical characteristics, protein-protein interactions, subcellular locations, anticipated active sites, secondary and tertiary structures, allergenicity, antigenicity, and toxicity properties. The protein has significant active amino acid residues with no allergenicity, elevated antigenicity, and no toxicity.

SCK종양 세포에서Stress Protein의 합성유도 (Induction of Stress Proteins in the SCK Tumor Cells)

  • 강만식;김경희
    • 한국동물학회지
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    • 제31권3호
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    • pp.157-164
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    • 1988
  • SCK종양세포에 온열처리와 여러가지 sulihydryl-reacting agents을 처리하여 stress protein의 합성을 유도하고, 그 양상을 검토해 봄으로서 stress proteins의 합성유도와 denatured protein의 생성과의 관계를 고찰하였다. 세포에 cycloximid와 더불어 Zn또는 ME를 처리한 경우에는 stress protein의 합성이 일어나지 않았으나,온열처리 또는 IAA를 처리한 경우에는 stress protein의 합성이 유도되었다. 이 결과로 미루어 볼 때,stress protein의 유도 경로에는 두 가지가 있어서 새로운 단백질의 합성이 필요한 경로와 새로운 단백질의 합성과는 무관한 경로가 있는 것으로 추정할 수 있었다. 결국, 본 실험에서 사용한 stress들이 기존의 mature protein을 denature시키거나 (온열처리 또는 IAA),새로 합성된 immature protein을 denatur시키는 것,(Zn 또는 ME)으로 알려져 있으므로,stress에 의한 abnormal protein의 출현이 stress proteins의 합성을 유도하는 tigger의 구실을 하는 것으로 생각된다. 이 밖에 여러 가지 stress가 동시에 작용할 경우, 세포는 보다 강한 stress에 대해서 stress protein을 합성하여 대치하게 되는 것으로 생각된다.

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Identification of a mimotope of an infectious bronchitis virus S1 protein

  • Zhou, Jingming;Li, Jianan;Li, Yanghui;Liu, Hongliang;Qi, Yanhua;Wang, Aiping
    • Journal of Veterinary Science
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    • 제22권4호
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    • pp.49.1-49.6
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    • 2021
  • The S1 protein of the infectious bronchitis virus (IBV) is a major structural protein that induces the production of the virus-neutralization antibodies. The monoclonal antibody against the IBV M41 S1 protein was used as a target for biopanning. After three rounds of biopanning, randomly selected phages bound to the monoclonal antibody. Sequence analysis showed that the dominant sequence was SFYDFEMQGFFI. Indirect competitive enzyme-linked immunosorbent assay showed that SFYDFEMQGFFI is a mimotope of the S1 protein that was predicted by PepSurf. The mimotope may provide information for further structural and functional analyses of the S1 protein.

Effect of S100A8 and S100A9 on expressions of cytokine and skin barrier protein in human keratinocytes

  • MUN JEONG KIM;MI AE IM;JI‑SOOK LEE;JI YOUNG MUN;DA HYE KIM;AYOUNG GU;IN SIK KIM
    • Molecular Medicine Reports
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    • 제20권3호
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    • pp.2476-2483
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    • 2019
  • Atopic dermatitis (AD ) is an inflammatory skin disorder caused by immunological dysregulation and genetic factors. Whether the expression levels of cytokine and skin barrier protein were altered by S100 calcium binding protein A8 (S100A8) and S100A9 in human keratinocytic HaCaT cells was examined in the present study. Alterations of cytokine expression were examined by ELI SA following treatment with S100A8/9 and various signal protein-specific inhibitors. Activation of the mitogen activated protein kinase (MAPK) pathway and nuclear factor (NF)-κB was evaluated by using western blotting and an NF-κB activity test, respectively. The expression levels of interleukin (IL )-6, IL- 8 and monocyte chemoattractant protein-1 increased following treatment with S100A8 and S100A9, and the increase was significantly blocked by specific signaling pathway inhibitors, including toll-like receptor 4 inhibitor (TLR 4i), rottlerin, PD98059, SB203580 and BAY-11-7085. Extracellular signal-regulated kinase (ER K) and p38 MAPK pathways were activated in a time-dependent manner following treatment with S100A8 and S100A9. Phosphorylation of ER K and p38 MAPK were blocked by TLR 4i and rottlerin. S100A8 and S100A9 induced translocation of NF-κB in a time-dependent manner, and the activation of NF-κB was inhibited by TLR 4i, rottlerin, PD98059 and SB203580. In addition, S100A8 and S100A9 decreased the expression of skin barrier proteins, filaggrin and loricrin. These results may help to elucidate the pathogenic mechanisms of AD and develop clinical strategies for controlling AD.

항인지질증후군에서 S단백질 결핍증에 대한 연구 (A Study of Protein S Deficiency in Antiphospholipid Syndrome)

  • 남윤성;김남근;강명서;오도연;차광열
    • Clinical and Experimental Reproductive Medicine
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    • 제28권2호
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    • pp.105-110
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    • 2001
  • Objective: To evaluate the abnormality of protein S in patients with recurrent spontaneous abortion due to antiphospholipid syndrome. Material and Method: Antigen and activity of protein S were analyzed by enzyme immunoassay and clotting method, respectively. Results: Of 18 patients with antiphospholipid syndrome, 4 patients were found to have no abnormality of protein S. There were 14 cases of protein S abnormality. Among them, there were 8 cases of type 1, 1 case of type 2, and 5 cases of type 3 protein S deficiency. Conclusion: So in the workup of patients with recurrent spontaneous abortion due to antiphospholipid syndrome, the evaluation for protein S is required.

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