| Bicine is an organic compound used as a buffering agent. It is one of Good's buffers and has a pKa of 8.35 at 20 °C. It is prepared by the reaction of glycine with ethylene oxide, followed by hydrolysis of the resultant lactone.
Bicine is a contaminant in amine systems used for gas sweetening. It is formed by amine degradation in the presence of O2, SO2, H2S or Thiosulfate. |
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| InChI=1S/C6H13NO4/c8-3-1-7(2-4-9)5-6(10)11/h8-9H,1-5H2,(H,10,11) |
| FSVCELGFZIQNCK-UHFFFAOYSA-N |
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Good's buffer substance
Any member of a collection of zwitterionic buffer substances selected or devised for suitability in experimental biological systems according to a number of predetermined criteria. Named after Dr. Norman Good.
(via bicine )
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View more via ChEBI Ontology
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N,N-bis(2-hydroxyethyl)glycine
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Bicine
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ChemIDplus
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bicine buffer
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ChEBI
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150-25-4
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CAS Registry Number
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ChemIDplus
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1769362
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Beilstein Registry Number
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Beilstein
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1769362
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Reaxys Registry Number
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Reaxys
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3532
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Gmelin Registry Number
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Gmelin
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Choi SP, Park YC, Lee J, Sim SJ, Chang HN (2012)
Effects of L-arginine on refolding of lysine-tagged human insulin-like growth factor 1 expressed in Escherichia coli.
Bioprocess and biosystems engineering 35, 255-263 [PubMed:22002161]
[show Abstract]
Insulin-like growth factor 1 (IGF1), a therapeutic protein, is highly homologous to proinsulin in 3-dimensional structure. To highly express IGF1 in recombinant Escherichia coli, IGF1 was engineered to be fused with the 6-lysine tag and ubiquitin at its N-terminus (K6Ub-IGF1). Fed-batch fermentation of E. coli TG1/pAPT-K6Ub-IGF1 resulted in 60.8 g/L of dry cell mass, 18% of which was inclusion bodies composed of K6Ub-IGF1. Subsequent refolding processes were conducted using accumulated inclusion bodies. An environment of 50 mM bicine buffer (pH 8.5), 125 mM L-arginine, and 4 °C was chosen to optimize the refolding of K6Ub-IGF1, and 240 mg/L of denatured K6Ub-IGF1 was refolded with a 32% yield. The positive effect of L-arginine on K6Ub-IGF1 refolding might be ascribed to preventing unfolded K6Ub-IGF1 from undergoing self-aggregation and thus increasing its solubility. The simple dilution refolding, followed by cleavage of the fusion protein by site-specific UBP1 and chromatographic purification of IGF1, led production of authentic IGF1 with 97% purity and an 8.5% purification yield, starting from 500 mg of inclusion bodies composed of K6Ub-IGF1, as verified by various analytical tools, such as RP-HPLC, CD spectroscopy, MALDI-TOF mass spectrometry, and Western blotting. Thus, it was confirmed that L-arginine with an aggregation-protecting ability could be applied to the development of refolding processes for other inclusion body-derived proteins. |
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