Aptamer-Modified Magnetic Beads in Affinity Separation of Proteins

2015 ◽  
pp. 67-82 ◽  
Author(s):  
Guohong Zhu ◽  
Johanna-Gabriela Walter
Keyword(s):  
Magnetic Beads ◽  
Affinity Separation ◽  
Separation Of Proteins

scholarly journals Preparation of nanogel-immobilized porous gel beads for affinity separation of proteins: fusion of nano and micro gel materials

2014 ◽  
Vol 47 (2) ◽  
pp. 220-225 ◽  
Author(s):  
Yu Hoshino ◽  
Yuka Arata ◽  
Yusuke Yonamine ◽  
Shih-Hui Lee ◽  
Aki Yamasaki ◽  
...  
Keyword(s):  
Affinity Separation ◽  
Gel Beads ◽  
Separation Of Proteins

Affinity Separation of Proteins in Aqueous Two-Phase Systems

1990 ◽  
pp. 335-344 ◽  
Author(s):  
T. Franco ◽  
B. A. Andrews ◽  
O. Cascone ◽  
C. Hodgson ◽  
A. T. Andrews ◽  
...  
Keyword(s):  
Affinity Separation ◽  
Two Phase ◽  
Aqueous Two Phase Systems ◽  
Phase Systems ◽  
Separation Of Proteins

Affinity Separation of Nucleic Acids on Monosized Magnetic Beads

1993 ◽  
pp. 479-485
Author(s):  
Mathias Uhlén ◽  
Ørjan Olsvik ◽  
Erik Hornes
Keyword(s):  
Nucleic Acids ◽  
Magnetic Beads ◽  
Affinity Separation

Affinity separation of proteins in aqueous three-phase systems

1988 ◽  
Vol 175 (1) ◽  
pp. 154-161 ◽  
Author(s):  
Per-Åke Albertsson ◽  
Gerd Birkenmeier
Keyword(s):  
Affinity Separation ◽  
Three Phase ◽  
Phase Systems ◽  
Separation Of Proteins

Synthesis of petal-like ferric oxide/cysteine architectures and their application in affinity separation of proteins

2014 ◽  
Vol 34 ◽  
pp. 468-473 ◽  
Author(s):  
Xueyan Zou ◽  
Kun Li ◽  
Yanbin Yin ◽  
Yanbao Zhao ◽  
Yu Zhang ◽  
...  
Keyword(s):  
Ferric Oxide ◽  
Affinity Separation ◽  
Separation Of Proteins

Ni2+-zeolite/ferrosphere and Ni2+-silica/ferrosphere beads for magnetic affinity separation of histidine-tagged proteins

2016 ◽  
Vol 45 (4) ◽  
pp. 1582-1592 ◽  
Author(s):  
T. A. Vereshchagina ◽  
M. A. Fedorchak ◽  
O. M. Sharonova ◽  
E. V. Fomenko ◽  
N. N. Shishkina ◽  
...  
Keyword(s):  
Recombinant Proteins ◽  
Shell Structure ◽  
Magnetic Beads ◽  
Core Shell ◽  
Affinity Separation ◽  
High Affinity ◽  
Core Shell Structure

Ferrosphere-based magnetic beads of a core–shell structure with immobilized Ni2+ having a high affinity towards His-tagged recombinant proteins were fabricated.

scholarly journals Functionalized Nano-adsorbent for Affinity Separation of Proteins

2018 ◽  
Vol 13 (1) ◽  
Author(s):  
Xueyan Zou ◽  
Fengbo Yang ◽  
Xin Sun ◽  
Mingming Qin ◽  
Yanbao Zhao ◽  
...  
Keyword(s):  
Affinity Separation ◽  
Separation Of Proteins ◽  
Nano Adsorbent

Polymer Nanoparticles Covered with Phosphorylcholine Groups and Immobilized with Antibody for High-Affinity Separation of Proteins

2008 ◽  
Vol 9 (3) ◽  
pp. 828-833 ◽  
Author(s):  
Yusuke Goto ◽  
Ryosuke Matsuno ◽  
Tomohiro Konno ◽  
Madoka Takai ◽  
Kazuhiko Ishihara
Keyword(s):  
Polymer Nanoparticles ◽  
Affinity Separation ◽  
High Affinity ◽  
Separation Of Proteins

scholarly journals The trans-Acting Protein Interacting with the DNA Motif Proximal to the Transcriptional Start Site of Plant l-Asparaginase Is Bacterial Sarcosine Oxidase

2004 ◽  
Vol 186 (3) ◽  
pp. 811-817 ◽  
Author(s):  
William T. Jones ◽  
Taha Al-Samarrai ◽  
Janice M. Reeves ◽  
Gordon B. Ryan ◽  
Christopher A. Kirk ◽  
...  
Keyword(s):  
Magnetic Beads ◽  
Transcriptional Start Site ◽  
Sequence Motif ◽  
Start Site ◽  
Affinity Separation ◽  
Specific Sequence ◽  
Repressor Protein ◽  
Α Subunit ◽  
Sarcosine Oxidase ◽  
Gel Retardation

ABSTRACT A trans-acting protein interacting with a specific sequence motif proximal to the transcriptional start site of the l-asparaginase promoter has been observed previously (E. Vincze, J. M. Reeves, E. Lamping, K. J. F. Farnden, and P. H. S. Reynolds, Plant Mol. Biol. 26:303-311, 1994). Gel retardation experiments in which protein extracts of Mesorhizobium loti and developing nodules were used suggested a bacterial origin for the repressor binding protein (rep2037). Nodulation tests were performed by using different Fix− Tn5 mutants of M. loti. Analyses of these mutants revealed a correlation between the presence of Mesorhizobium in the nodule-like structures and the ability of nodule protein extracts to bind the repressor binding domain (RBD). Through the use of mutated RBD sequences, the RBD sequence was identified as CTAAAAT. The repressor protein was isolated from M. loti NZP2037 by multiple chromatographic procedures and affinity separation by using concatemers of RBD attached to magnetic beads. Sequencing of the recovered protein resulted in identification of the repressor protein as the sarcosine oxidase α subunit. This was confirmed by expression of the gene encoding the M. loti α subunit of sarcosine oxidase in Escherichia coli. When the expressed peptide was bound to RBD, the gel retardation result was identical to the result obtained with rep2037 from M. loti strain NZP2037.

Sign in / Sign up

Export Citation Format

Share Document