Detail of "5961-85-3"

Reference

Genetically engineered binding proteins as biosensors for fermentation and cell culture

Genetically engineered binding proteins as biosensors for fermentation and cell culture. Ge, Xudong; Tolosa, Leah; Simpson, Jen; Rao, Govind (Department of Chemical and Biochemical Engineering, University of Maryland, Baltimore, MD 21250, USA). Biotechnology and Bioengineering, 84(6), 723-731 (English) 2003 John Wiley & Sons, Inc. CODEN: BIBIAU. ISSN: 0006-3592. DOCUMENT TYPE: Journal CA Section: 16 (Fermentation and Bioindustrial Chemistry) The signal-transduction properties and the potential applications of two engineered binding proteins from E. coli were extensively studied. Both proteins have a single cysteine mutation in their polypeptide chains, which allow the introduction of an environmentally sensitive fluorophore: ANS for glucose-binding protein (GBP) and acrylodan for glutamine-binding protein (QBP). Both proteins respond to their ligands in the micromolar range. The proteins can be stored at 4°C for at least 5 mo. Apparent binding const., protein concn., and fluorophore are three major factors that affect the biosensor's responsive ranges. The binding of the ligand is quick and reversible in soln., but the unfavorable dissocn. equil. and mass-transfer resistance for encapsulated proteins can delay the response to several minutes and the recovery to hours. Simulated results show that using dialysis tubing with a diam. of 1 mm or less is possible to reduce the recovery time to less than 30 min. The potential applications of GBP were studied in yeast fermn. and E. coli fermns. in three different scales: 150 mL, 5 mL, and 100 mL. The results were compared with an YSI 2700 Chem. Analyzer. 5961-85-3 and 57450-03-0 which are cas registry numbers of chemicals are mentioned. Although the latter could not give reliable results for the E. coli fermns. as the glucose concn. in LB medium is close to its lower detection limit, the glucose biosensor presented here was successfully applied to each situation. Glutamine-binding protein was tested in cell cultures of two different scales (100 mL and 100 mL) and the results were also compared with those obtained with YSI. Both QBP and YSI gave good results for the 100-mL cell culture, but the relatively large sample vol. requirement of YSI (at least 5 mL) prevented it from being used in the 100-mL cell culture. Because of their small sample vol. requirements (less than 1 mL) and high sensitivity, the assays described here might find wide applications in high-throughput bioprocessing. .

Methods for biomarker discovery and diagnostic screening

All Rights Reserved. Methods for biomarker discovery and diagnostic screening. Warder, Scott E.; Tucker, Lora A.; McKeegan, Evelyn Mary; Strelitzer, Tamara J.In this study， 9001-50-7 and 5961-85-3 are also used. (USA ). U.S. Pat. Appl. Publ. US 2007015911 A1 18 Jan 2007,27pp., Cont.-in-part of U.S. Ser. No. 96,168, abandoned. (English). (United States of America). CODEN: USXXCO. INCL: 530414000. APPLICATION: US 2006-486233 13 Jul 2006. PRIORITY: US 2005-96168 31 Mar 2005. DOCUMENT TYPE: Patent CA Section: 9 (Biochemical Methods) Section cross-reference(s): 14 The subject invention relates to methods of profiling biomols. from mammalian biol. samples, for example, plasma or serum, in order to discover markers of disease, treatment, toxicity or efficacy. The resulting profiles may be used, for instance, to discover novel markers or patterns that may be used to classify samples into groups, for example, disease vs. normal, responders vs. non-responders, or to stratify patients for clin. trials. In the methods, the biol. specimen is reacted with a reducing agent to form a ppt. and the treated specimen is analyzed. The reducing agent treatment of plasma or serum samples from human and mice revealed a significant increase in the no. of peaks obsd. in MALDI-MS spectra and in their reproducibility. Reducing agent treatment depleted albumin and other high-abundant proteins. .