- 関
- recombinant、recombination、recombinational、recombinogenic
WordNet
- of or relating to recombinant DNA
- a cell or organism in which genetic recombination has occurred
PrepTutorEJDIC
- 遺伝子の新結合による
UpToDate Contents
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English Journal
- Assessment of naturally occurring covalent and total dimer levels in human IgG1 and IgG2.
- Yang J1, Goetze AM1, Flynn GC2.Author information 1Department of Process and Product Development, Amgen Inc., Thousand Oaks, 91320, United States.2Department of Process and Product Development, Amgen Inc., Thousand Oaks, 91320, United States. Electronic address: gflynn@amgen.com.AbstractAntibody dimers, two self-associated monomers, have been detected on both recombinantly expressed and endogenous human IgG proteins. Nearly 10 years ago, Yoo et al. (2003) described low levels of IgG2 covalent dimer, in human serum, but did not quantify the levels. Here we quantify the total and covalent dimer levels of IgG2 and IgG1 in human blood, and study the origin of covalent dimer formation. Low levels (<1%) of total IgG1 and IgG2 dimers were measured in freshly prepared human plasma. Both IgG1 and IgG2 covalent dimers were also found in plasma. Whereas IgG1 covalent dimer levels were significantly reduced by steps intended to eliminate artifacts during sample preparation, IgG2 covalent dimer levels remain stable in such conditions. About 0.4% of IgG2 in plasma was in a covalent dimer form, yet very little (<0.03%) of IgG1 covalent dimer could be considered naturally occurring. IgG2 dimer also formed in vitro under conditions designed to mimic those in blood, suggesting that formation occurs in vivo during circulation. Thus, small amounts of covalent IgG2 dimer do appear to form naturally.
- Molecular immunology.Mol Immunol.2014 Mar;58(1):108-15. doi: 10.1016/j.molimm.2013.11.011. Epub 2013 Dec 8.
- Antibody dimers, two self-associated monomers, have been detected on both recombinantly expressed and endogenous human IgG proteins. Nearly 10 years ago, Yoo et al. (2003) described low levels of IgG2 covalent dimer, in human serum, but did not quantify the levels. Here we quantify the total and cov
- PMID 24321397
- Kinetic and structural characterization of an alternatively spliced variant of human mitochondrial 5'(3')-deoxyribonucleotidase.
- Pachl P, Fábry M, Veverka V, Brynda J, Rezáčová P.Author information Institute of Organic Chemistry and Biochemistry and.AbstractAbstract Human mitochondrial 5'(3')-deoxyribonucleotidase (mdN) catalyzes dephosphorylation of nucleoside monophosphates, and thus helps maintain homeostasis of deoxynucleosides required for mitochondrial DNA synthesis. Mature mdN is a 23-kDa dimeric protein with highest expression levels in the heart, brain and skeletal muscle. We have identified an alternative splice variant of the mdN gene containing an 18-nucleotide insertion encoding 6 amino acids (GKWPAT) at the 3'-end of the penultimate exon 4. We recombinantly expressed this enzyme variant and characterized its biochemical and kinetic properties as well as its three-dimensional structure. Our high-resolution (1.27 Å) crystal structure revealed that the insertion forms a loop located in the vicinity of the active site pocket and affects enzyme kinetic parameters as well as protein thermal stability.
- Journal of enzyme inhibition and medicinal chemistry.J Enzyme Inhib Med Chem.2014 Feb 10. [Epub ahead of print]
- Abstract Human mitochondrial 5'(3')-deoxyribonucleotidase (mdN) catalyzes dephosphorylation of nucleoside monophosphates, and thus helps maintain homeostasis of deoxynucleosides required for mitochondrial DNA synthesis. Mature mdN is a 23-kDa dimeric protein with highest expression levels in the hea
- PMID 24506201
- Identification and characterization of a galacturonic acid transporter from Neurospora crassa and its application for Saccharomyces cerevisiae fermentation processes.
- Benz JP, Protzko RJ, Andrich JM, Bauer S, Dueber JE, Somerville CR.AbstractBACKGROUND: Pectin-rich agricultural wastes potentially represent favorable feedstocks for the sustainable production of alternative energy and bio-products. Their efficient utilization requires the conversion of all major constituent sugars. The current inability of the popular fermentation host Saccharomyces cerevisiae to metabolize the major pectic monosaccharide D-galacturonic acid (D-GalA) significantly hampers these efforts. While it has been reasoned that the optimization of cellular D-GalA uptake will be critical for the engineering of D-GalA utilization in yeast, no dedicated eukaryotic transport protein has been biochemically described. Here we report for the first time such a eukaryotic D-GalA transporter and characterize its functionality in S. cerevisiae.
- Biotechnology for biofuels.Biotechnol Biofuels.2014 Feb 6;7(1):20. [Epub ahead of print]
- BACKGROUND: Pectin-rich agricultural wastes potentially represent favorable feedstocks for the sustainable production of alternative energy and bio-products. Their efficient utilization requires the conversion of all major constituent sugars. The current inability of the popular fermentation host Sa
- PMID 24502254
Japanese Journal
- Biochemical characterization of L-arabitol 2-dehydrogenase from Pantoea ananatis(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
- Sakakibara Yoshikiyo,Torigoe Kyoko
- Journal of bioscience and bioengineering 113(6), 715-718, 2012-06
- … LAD, whose endogenous substrate was unknown, was recombinantly prepared and biochemically analyzed. …
- NAID 110009470591
- Ralstonia sp. U2 naphthalene dioxygenase and Comamonas sp. JS765 nitrobenzene dioxygenase show differences in activity towards methylated naphthalenes(MICROBIAL PHYSIOLOGY AND BIOTECHNOLOGY)
- Tondervik Anne,Bruheim Per,Berg Laila [他],Ellingsen Trond E.,Kotlar Hans K.,Valla Svein,Throne-Holst Mimmi
- Journal of bioscience and bioengineering 113(2), 173-178, 2012-02
- … Here we show that recombinantly produced NDO from Raistonia sp. …
- NAID 110009418664
- PhAP protease from Pseudoalteromonas haloplanktis TAC125: Gene cloning, recombinant production in E. coli and enzyme characterization
- D. de Pascale,M. Giuliani,C. De Santi,N. Bergamasco,A. Amoresano,A. Carpentieri,E. Parrilli,M.L. Tutino
- Polar science 4(2), 285-294, 2010-08
- 南極の海洋性バクテリアであるPseudoalteromonas haloplanktis TAC125により生産される細胞外酵素について、タンパク質分解酵素の低温適応を調べた。プロテオミクス解析により、その培養液の上澄みからいくつかのタンパク分解活性を同定した。以後の解析にはPhAPプロテアーゼを選び、その遺伝子をクローニングして遺伝子組み換え技術を用い、大腸菌細胞中で生産させた。得られたプロテア …
- NAID 110007702238
Related Links
- 2002, Gilbert S. Banker & Christopher T. Rhodes, Modern Pharmaceutics, 4th edition, Informa Health Care, ISBN 0824706749, page 699: One of the first examples of the immunogenicity of recombinantly derived ...
- Definition of recombinantly in the Definitions.net dictionary. Meaning of recombinantly. What does recombinantly mean? Information and translations of recombinantly in the most comprehensive dictionary definitions resource on the ...
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★リンクテーブル★
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- 英
- recombination、recombinant、recombinational、recombinogenic、recombinantly
- 関
- 組換え型、組換え性、組換え体、再結合、リコンビナント、組換え産物、組換え誘導
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- 関
- recombinant、recombinantly、recombination、recombinational
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- 関
- recombinant、recombinantly、recombination、recombinogenic
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- 関
- recombinantly、recombination、recombinational、recombinogenic