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publisher: Biotech Patent News, published: 2004-12-01
ASIN: B00081Y82M
This digital document is an article from BIOTECH Patent News, published by Biotech Patent News on December 1, 2004. The length of the article is 1352 words. The page length shown above is based on a typical 300-word page. The article is delivered in HTML format and is available in your Amazon.com Digital Locker immediately after purchase. You can view it with any web browser.
Citation Details Title: Chromos enters into agreement with Pfizer to develop cell lines for production of recombinant proteins.(Chromos Molecular Systems) Publication: BIOTECH Patent News (Newsletter) Date: December 1, 2004 Publisher: Biotech Patent News Volume: 18 Issue: 12
Distributed by Thomson Gale
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by: C.L. Qiao
publisher: Elsevier, published: 2006-09-01
ASIN: B000PBZRFW
This digital document is a journal article from International Biodeterioration & Biodegradation, published by Elsevier in 2006. The article is delivered in HTML format and is available in your Amazon.com Media Library immediately after purchase. You can view it with any web browser.
Description: High-density culture was achieved through controlling specific growth rate by limiting glucose concentration to <0.2gL^-^1. Carboxylesterase B1 capable of hydrolyzing organophosphate esters was purified from Escherichia coli strain BL21 carrying a cloned esterase B1 gene from mosquito. The recombinant strain BL21 carrying pET-ESTB1 was used for the fermentation. Product formation was induced by either a temperature shift from 30 to 42^oC or by feeding a mixture of glucose and lactose. Cell growth and production of detoxifying enzyme were affected by oxygen availability. The maximum biomass of E. coli BL21 (pET-ESTB1) increased from 14.9 to 31.5gdry cell weightl^-^1. Using the host strain E. coli BL21 (DE3), detoxifying enzyme was over-expressed at a biomass level of up to 31.5gdry weightl^-^1. The enzyme had a molecular mass of 64kDa, its optimum temperature was approx. 37^oC; at pH 7 the relative activity after 3h was 85.9% at 28^oC, 64.9% at 34^oC, and 4.5% at 40^oC. The enzyme activity of cells grown at lower temperatures was much higher; at 18^oC it almost twice than at 20 or 22^oC.
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by: Unavailable
publisher: Biotech Patent News, published: 2009-01-01
ASIN: B002C29M1C
This digital document is an article from BIOTECH Patent News, published by Biotech Patent News on January 1, 2009. The length of the article is 383 words. The page length shown above is based on a typical 300-word page. The article is delivered in HTML format and is available immediately after purchase. You can view it with any web browser.
Citation Details Title: Bone Biologics Announces Major United States Patent Issuances for Its Recombinant Protein Process. Author: Unavailable Publication: BIOTECH Patent News (Newsletter) Date: January 1, 2009 Publisher: Biotech Patent News Volume: 23 Issue: 1
Distributed by Gale, a part of Cengage Learning
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by: Dian-Xiang Li
publisher: Science Publications, published: 2010-06-22
ASIN: B0047V4JAU
This digital document is an article from American Journal of Biochemistry and Biotechnology, published by Science Publications on June 22, 2010. The length of the article is 3272 words. The page length shown above is based on a typical 300-word page. The article is delivered in HTML format and is available immediately after purchase. You can view it with any web browser.
From the author: Key words: Fenneropenaeus chinensis, recombinant Fc-COMT, VA, HPLC-MS
Citation Details Title: Expression, purification and activity assay of the recombinant protein of Catechol-O-Methyltransferase from Chinese white shrimp (Fenneropenaeus chinensis).(Report) Author: Dian-Xiang Li Publication: American Journal of Biochemistry and Biotechnology (Magazine/Journal) Date: June 22, 2010 Publisher: Science Publications Volume: 6 Issue: 3 Page: 148(7)
Article Type: Report
Distributed by Gale, a part of Cengage Learning
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by: Laird Harrison
publisher: International Medical News Group, published: 2010-12-01
ASIN: B004I8TWE0
This digital document is an article from Pediatric News, published by International Medical News Group on December 1, 2010. The length of the article is 689 words. The page length shown above is based on a typical 300-word page. The article is delivered in HTML format and is available immediately after purchase. You can view it with any web browser.
Citation Details Title: Variety of therapies in pipeline for food allergies: desensitization, anti-immunoglobulin tx, and engineered recombinant proteins being studied.(CLINICAL ROUNDS) Author: Laird Harrison Publication: Pediatric News (Magazine/Journal) Date: December 1, 2010 Publisher: International Medical News Group Volume: 44 Issue: 12 Page: 29(1)
Distributed by Gale, a part of Cengage Learning
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publisher: Springer, published: 2006-09-18
ASIN: 0387303480
EAN: 9780387303482
sales rank: 2924792
This volume is a collection of a variety of brain proteins and peptides whose structures and functions are relatively well known. Each chapter provides a succinct and up-to-date summary of a protein or peptide as well as a review of the individual's contributions to the field. The volume explores the progress that has been made in the field over the past few years and provides insight into the field today.
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publisher: CRC Press, published: 2003-02-05
ASIN: 0824707265
EAN: 9780824707262
sales rank: 3444891
This publication details the isolation of proteins from biological materials, techniques for solid-liquid separation, concentration, crystallization, chromatography, scale-up, process monitoring, product formulation, and regulatory and commercial considerations in protein production. The authors discuss the release of protein from a biological host, selectivity in affinity chromatography, precipitation of proteins (both non-specific and specific), extraction for rapid protein isolation, adsorption as an initial step for the capture of proteins, scale-up and commercial production of recombinant proteins, and process monitoring in downstream processing.
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publisher: Springer, published: 2010-11-29
ASIN: 1441921427
EAN: 9781441921420
sales rank: 8512085
This text provides an up-to-date collection of theoretical and experimental studies into protein folding, misfolding, aggregation, and stability. Additionally, issues faced during the development of protein products are illustrated. It contains an introductory chapter for readers new to the protein folding field. The book provides a thorough and clear discussion of computational approaches to understanding and modeling protein aggregation.
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publisher: Humana Press, published: 2002-04-15
ASIN: 0896036782
EAN: 9780896036789
sales rank: 2562369
Christoph Kannicht and a panel of highly experienced researchers describe readily reproducible methods for detecting and analyzing the posttranslational modifications of protein, particularly with regard to protein function, proteome research, and the characterization of pharmaceutical proteins. Among the methods presented are those for analyzing the assignment of disulfide bond sites in proteins, protein N-glycosylation and protein O-glycosylation, and oligosaccharides present at specific single glycosylation sites in a protein. Additional powerful techniques facilitate the analysis of glycosylphosphatidylinositols, lipid modifications, protein phosphorylation and sulfation, protein methylation and acetylation, a-amidation, g-glutamate, isoaspartate, and lysine hydroxylation.
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publisher: Springer, published: 2011-10-25
ASIN: 3642233716
EAN: 9783642233715
sales rank: 4392383
Fluorescent proteins are intimately connected to research in the life sciences. Tagging of gene products with fluorescent proteins has revolutionized all areas of biosciences, ranging from fundamental biochemistry to clinical oncology, to environmental research. The discovery of the Green Fluorescent Protein, its first, seminal application and the ingenious development of a broad palette of fluorescence proteins of other colours, was consequently recognised with the Nobel Prize for Chemistry in 2008. Fluorescent Proteins I is devoted to the basic photophysical and photochemical aspects of fluorescent protein technology. Experienced experts highlight colour tuning, the exploration of switching phenomena and respective methods for their investigation. The book provides a thorough understanding of primary molecular processes allowing the design of fluorescent proteins for specific applications.
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