• Title/Summary/Keyword: ProteinChip

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Influence of Yeast Fermented Cassava Chip Protein (YEFECAP) and Roughage to Concentrate Ratio on Ruminal Fermentation and Microorganisms Using In vitro Gas Production Technique

  • Polyorach, S.;Wanapat, M.;Cherdthong, A.
    • Asian-Australasian Journal of Animal Sciences
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    • v.27 no.1
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    • pp.36-45
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    • 2014
  • The objective of this study was to determine the effects of protein sources and roughage (R) to concentrate (C) ratio on in vitro fermentation parameters using a gas production technique. The experimental design was a $2{\times}5$ factorial arrangement in a completely randomized design (CRD). Factor A was 2 levels of protein sources yeast fermented cassava chip protein (YEFECAP) and soybean meal (SBM) and factor B was 5 levels of roughage to concentrate (R:C) ratio at 80:20, 60:40, 40:60, 20:80, and 0:100, respectively. Rice straw was used as a roughage source. It was found that gas production from the insoluble fraction (b) of YEFECAP supplemented group was significantly higher (p<0.05) than those in SBM supplemented group. Moreover, the intercept value (a), gas production from the insoluble fraction (b), gas production rate constants for the insoluble fraction (c), potential extent of gas production (a+b) and cumulative gas production at 96 h were influenced (p<0.01) by R:C ratio. In addition, protein source had no effect (p>0.05) on ether in vitro digestibility of dry matter (IVDMD) and organic (IVOMD) while R:C ratio affected the IVDMD and IVOMD (p<0.01). Moreover, YEFECAP supplanted group showed a significantly increased (p<0.05) total VFA and $C_3$ while $C_2$, $C_2:C_3$ and $CH_4$ production were decreased when compared with SBM supplemented group. In addition, a decreasing R:C ratio had a significant effect (p<0.05) on increasing total VFA, $C_3$ and $NH_3$-N, but decreasing the $C_2$, $C_2:C_3$ and CH4 production (p<0.01). Furthermore, total bacteria, Fibrobacter succinogenes, Ruminococcus flavefaciens and Ruminococcus albus populations in YEFECAP supplemented group were significantly higher (p<0.05) than those in the SBM supplemented group while fungal zoospores, methanogens and protozoal population remained unchanged (p>0.05) as compared between the two sources of protein. Moreover, fungal zoospores and total bacteria population were significantly increased (p<0.01) while, F. succinogenes, R. flavefaciens, R. albus, methanogens and protozoal population were decreased (p<0.01) with decreasing R:C ratio. In conclusion, YEFECAP has a potential for use as a protein source for improving rumen fermentation efficiency in ruminants.

Microbead based micro total analysis system for Hepatitis C detection (마이크로비드를 이용한 초소형 C형 간염 검출 시스템의 제작)

  • Sim, Tae-Seok;Lee, Bo-Rahm;Lee, Sang-Myung;Kim, Min-Soo;Lee, Yoon-Sik;Kim, Byung-Gee;Kim, Yong-Kweon
    • Proceedings of the KIEE Conference
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    • 2006.07c
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    • pp.1629-1630
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    • 2006
  • This paper describes a micro total analysis system ($\mu$ TAS) for detecting and digesting the target protein which includes a bead based temperature controllable microchip and computer based controllers for temperature and valve actuation. We firstly combined the temperature control function with a bead based microchip and realized the on-chip sequential reactions using two kinds of beads. The PEG-grafted bead, on which RNA aptamer was immobilized, was used for capturing and releasing the target protein. The target protein can be chosen by the type of RNA aptamer. In this paper, we used the RNA aptamer of HCV replicase. The trypsin coated bead was used for digesting the released protein prior to the matrix assisted laser desorption ionization time of flight mass spectrometer (MALDI TOF MS). Heat is applied for release of the captured protein binding on the bead, thermal denaturation and trypsin digestion. PDMS microchannel and PDMS micro pneumatic valves were also combined for the small volume liquid handling. The entire procedures for the detection and the digestion of the target protein were successfully carried out on a microchip without any other chemical treatment or off-chip handling using $20\;{\mu}l$ protein mixture within 20 min. We could acquire six matched peaks (7% sequence coverage) of HCV replicase.

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Differential Protein and Gene Expression after Adenovirus-Mediated p16 Gene Transfer in Human Non-Small Cell Lung Cancer Cells

  • Park, Mi-Sun;Kang , Ho-Il;Jee, Seung-Wan;Lim, Si-Nae;Pyo, Jae-Hee;Eom , Mi-Ok;Ryeom , Tai-Kyung;Kim, Ok-Hee
    • Proceedings of the PSK Conference
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    • 2002.10a
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    • pp.291.2-291.2
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    • 2002
  • For the safety evaluation of adenovirus-mediated gene therapy. we have investigated gene and protein expression after transduction of adenoviral vector (Ad5CMV-p16) which contains tumor suppressor gene. p161NK4$\alpha$ in human non-small cell lung cancer (A549) cells. We compared the differential gene expression level in the A549 cells treated with Ad5CMV (null type) and Ad5CMV-p16 virus. respectively. by using cDNA membrane chip and oligonucleotide chip. (omitted)

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Single C-Reactive Protein Molecule Detection on a Gold-Nanopatterned Chip Based on Total Internal Reflection Fluorescence

  • Heo, Yunmi;Lee, Seungah;Lee, Sang-Won;Kang, Seong Ho
    • Bulletin of the Korean Chemical Society
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    • v.34 no.9
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    • pp.2725-2730
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    • 2013
  • Single C-reactive protein (CRP) molecules, which are non-specific acute phase markers and products of the innate immune system, were quantitatively detected on a gold-nanopatterned biochip using evanescent field-enhanced fluorescence imaging. The $4{\times}5$ gold-nanopatterned biochip (spot diameter of 500 nm) was fabricated by electron beam nanolithography. Unlabeled CRP molecules in human serum were identified with single-molecule sandwich immunoassay by detecting secondary fluorescence generated by total internal reflection fluorescence (TIRF) microscopy. With decreased standard CRP concentrations, relative fluorescence intensities reduced in the range of 33.3 zM-800 pM. To enhance fluorescence intensities in TIRF images, the distance between biochip surface and CRP molecules was optimally adjusted by considering the quenching effect of gold and the evanescent field intensity. As a result, TIRF only detected one single-CRP molecule on the biochip the first time.