Effects of propyl gallate on interaction between TNF-alpha and sTNFR-I using an affinity biosensor1

Li, Jing; Huang, Jiadong; Wu, Baoyan; Chen, Qiang

doi:10.1111/j.1745-7254.2005.00198.x

Cited by 4 publications

(1 citation statement)

References 28 publications

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“…Four hundred arc seconds of human renin were coupled on the cuvette of the IAsys plus biosensor. According to the method described by Li et al (14), the amount of immobilized renin was calculated as 2.45 pmol. The prepared soluble microsomal fraction of fat body expressed hPRR and the hemolymph expressed hPRR−ΔTMΔCD were diluted to 3 mg/ml and injected into the renin immobilized cuvette.…”

Section: Resultsmentioning

confidence: 99%

Binding affinity of full-length and extracellular domains of recombinant human (pro)renin receptor to human renin when expressed in the fat body and hemolymph of silkworm larvae

Kato

Suzuki

Park

2009

Journal of Bioscience and Bioengineering

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Transmembrane domains of some receptors have been found to be very important in the process of constitutive oligomerization, and in the stability and functioning of the receptor. In this study, full-length of human (pro)renin receptor (hPRR) and hPRR lacking cytoplasmic domain (hPRR-DeltaCD) were expressed in fat body of silkworm larvae, and the extracellular domain of hPRR (hPRR-DeltaTMDeltaCD) in hemolymph. Three forms of hPRR were used for investigation of the interaction between receptor and ligand using surface plasmon resonance (SPR). As a result, the cytoplasmic domain was not an essential requirement for binding affinity, but the transmembrane domain of hPRR was indispensable in the formation of functional hPRR. The dissociation equilibrium constants (K(D)) of purified hPRR and hPRR-DeltaCD were estimated to be 46 nM and 330 nM, respectively. No evidence of binding by the extracellular domain of hPRR located in hemolymph was found. However, the solubilized microsomal fraction of the extracellular domain of hPRR expressed in the fat body showed specific affinity, but lost its binding affinity after purification. Its binding affinity was recovered by mixing microsomal fraction of mock-injected fat body to the purified extracellular domain. It is probable that an artificial transmembrane domain stabilizes the extracellular domain of hPRR and native conformation may be structurally recovered. To our knowledge, these are the first findings describing the interaction of transmembrane and extracellular domains of hPRR with ligand and this may help towards the understanding of binding affinity of hPRR to ligand.

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Section: Resultsmentioning

confidence: 99%

Binding affinity of full-length and extracellular domains of recombinant human (pro)renin receptor to human renin when expressed in the fat body and hemolymph of silkworm larvae

Kato

Suzuki

Park

2009

Journal of Bioscience and Bioengineering

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Survey of the year 2005 commercial optical biosensor literature

2006

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We identified 1113 articles (103 reviews, 1010 primary research articles) published in 2005 that describe experiments performed using commercially available optical biosensors. While this number of publications is impressive, we find that the quality of the biosensor work in these articles is often pretty poor. It is a little disappointing that there appears to be only a small set of researchers who know how to properly perform, analyze, and present biosensor data. To help focus the field, we spotlight work published by 10 research groups that exemplify the quality of data one should expect to see from a biosensor experiment. Also, in an effort to raise awareness of the common problems in the biosensor field, we provide side-by-side examples of good and bad data sets from the 2005 literature.

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