Results 1 to 10 of about 216,985 (67)

Selection of imprinted nanoparticles by affinity chromatography [PDF]

, 2009
Soluble molecularly imprinted nanoparticles were synthesised via iniferter initiated polymerisation and separated by size via gel permeation chromatography.
Chianella, Iva, Guerreiro, A., Piletska, Elena V., Piletsky, Sergey A., Whitcombe, M. J.   +4 more
core   +1 more source

Pharmaceutical And Biomedical Applications Of Affinity Chromatography: Recent Trends And Developments [PDF]

, 2012
Affinity chromatography is a separation technique that has become increasingly important in work with biological samples and pharmaceutical agents. This method is based on the use of a biologically-related agent as a stationary phase to selectively ...
Alexandre, Allenmark, Arata, Bartolini, Basiaga, Bergstrom, Block, Block, Boonjob, Bouriotis, Bourne, Bowers-Komro, Brown, Calvano, Caspi, Cellar, Chaga, Chan, Chattopadhyay, Chen, Chen, Chen, Chen, Chen, Chen, Cheshev, Clarke, Clarke, Cong Bi, Conrad, Cuatrecasas, Dalgaard, David S. Hage, de Frutos M, de Paula, del Castillo, Denizli, Domenici, Dong, Duong-Thi, Efthimia Papastavros, Erika Pfaunmiller, Felix, Friedberg, Garberc-Porekar, Garberc-Porekar, German, Gould, Gustavsson, Gutiérrez, Hage, Hage, Hage, Hage, Hage, Hage, Hage, Hage, Hage, Haginaka, Hattori, Haupt, Hauri, Hermanson, Hjerten, Hodgson, Itakura, Iwaki, Jeanethe A. Anguizola, Jiang, John Vargas, Joseph, Joseph, Joseph, Joseph, Joseph, Jozwiak, Jozwiak, Jozwiak, Jozwiak, Kaliszan, Kalizan, Kim, Kim, Kim, Kitagawa, Kool, Kovarik, Kuester, Kullolli, Labrou, Labrou, Larsson, Lee, Lee, Lewinson, Li, Little, Liu, Liu, Liu, Loun, Loun, Loun, Lowe, Mairal, Mallia, Mallik, Mallik, Mallik, Mallik, Mancini, Matsuda, Mayer, Middle, Moaddel, Moaddel, Monzo, Moser, Moser, Mrabet, Nakamura-Tsuruta, Nakano, Nasal, Nelson, Nelson, Ng, Noctor, Noctor, Nuwaysir, Oates, Ohlson, Ohlson, Ohnmacht, Okanda, Oliveira, Panteghini, Patel, Patel, Pedersen, Peterson, Plavina, Porath, Potyrailo, QIAGEN Group, Qiu, Ren, Romig, Rong Li, Ryan Matsuda, Schiel, Schiel, Schiel, Schiel, Schreimer, Silver, Sing, Singhal, Slon-Usakiewicz, Soman, Stevenson, Strandh, Suksrichavalita, Tachibana, Takeda, Talbert, Thomas, Todorova, Tong, Tong, Tong, Turkova, Tweed, Uzun, Victor, Vivekananda, Vosseller, Walters, Wang, Wang, Wikstroem, Wilchek, Winzor, Wu, Xiwei Zheng, Xu, Xuan, Xuan, Yamamoto, Yang, Yang, Yang, Ye, Yoo, Yoo, Yoo, Yoo, Yoo, Zeng, Zeng, Zhao, Zhao   +201 more
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Purification of Mg2+-dependent phosphatidate phosphohydrolase from rat liver: new steps and aspects [PDF]

, 2005
A new procedure for the partial purification of Mg2+-dependent, N-ethylmaleimide-sensitive phosphatidate phosphohydrolase (Mg2+-PAP; EC 3.1.3.4) from rat liver cytosol is described, using protein precipitation with MgCl2, gel filtration on Sephacryl S ...
Butterwith, Cascales, DeMattos, Hopewell, Hosaka, Martin, Mavis, Minami, Nemoto, Nishida, Pollard   +10 more
core   +1 more source

A three-step purification of human α1-acid glycoprotein [PDF]

, 1984
α1-Acid glycoprotein (AGP) was purified to homogeneity by a 3-step procedure using pseudo-ligand affinity chromatography on immobilized Cibacron blue F3GA, Procion red HE3B, and preparative column isoelectric focusing.
Arnaud, Philippe, Bienvenu, Jacques, Laurent, Philippe, Miribel, Laurent, Vallve, Charles   +4 more
core   +1 more source

A Monomer-to-Trimer Transition of the Human Mitochondrial Transcription Termination Factor (mTERF) Is Associated with a Loss of in Vitro Activity [PDF]

, 2004
The human mitochondrial transcription termination factor (mTERF) is a nuclear-encoded 39-kDa protein that recognizes a mtDNA segment within the mitochondrial tRNALeu(UUR) gene immediately adjacent to and downstream of the 16 S rRNA gene. Binding of mTERF
Asin-Cayuela, Jordi, Attardi, Giuseppe, Helm, Mark   +2 more
core   +1 more source

Identification of novel components of Trypanosoma brucei editosomes [PDF]

, 2003
The editosome is a multiprotein complex that catalyzes the insertion and deletion of uridylates that occurs during RNA editing in trypanosomatids. We report the identification of nine novel editosome proteins in Trypanosoma brucei.
Carmean, Nicole, Ernst, Nancy L, Panigrahi, Aswini K, Salavati, Reza, Schnaufer, Achim, Stuart, Kenneth, Wang, Bingbing   +6 more
core   +2 more sources

Interaction of the 89K murine cytomegalovirus immediate-early protein with core histones [PDF]

, 1988
The conditions that permit the interaction of immediate-early proteins of murine cytornegalovirus (MCMV) with DNA were studied. Chromatography of extracts from infected cells on MCMV DNA cellulose and calf thymus DNA cellulose showed that pp89, the ...
Alberts, Bookout, Ebeling, Einck, Everett, Faber, Freeman, Green, Günther M. Keil, Hay, Hermiston, Isenberg, Kedes, Keil, Keil, Keil, Keil, Konrad Munch, Koszinowski, Koszinowski, Koszinowski, Kristie, Kristie, Martin Messerle, O'Hare, Ohlenbusch, Purifoy, Reddehase, Rigby, Stein, Tevethia, Ulrich H. Koszinowski, Weissbach   +32 more
core   +1 more source

Effects of antibodies against tubulin on the movement of reactivated sea urchin sperm flagella [PDF]

, 1980
Antibodies binding to sea urchin flagellar outer-doublet tubulin have been isolated from rabbit sera by tubulin-affinity chromatography employing electrophoretically purified tubulin as the immobilized substrate.
Asai, David J., Brokaw, Charles J.
core   +1 more source

Measurement of the Proteinase Inhibitors of the Bovine Pancreas by Radioimmunoassay [PDF]

, 1976
Bovine pancreas contains two polypeptide trypsin inhibitors that are not homologous and differ in their inhibitory activity towards chymotrypsin, kallikrein, elastase, and other serine proteinases. The Kunitz inhibitor and the Kazal inhibitor are present
Fink, Edwin, Greene, Lewis J., Peeters, H.   +2 more
core   +1 more source

The use of phenyl-Sepharose for the affinity purification of proteinases [PDF]

, 1993
Phenyl-Sepharose is most often used as an adsorbent for hydrophobic interaction chromatography (HIC). We report on its effective use for the affinity purification of some extracellular thermostable proteinases from bacterial sources.
Daniel, Roy M., Peek, Keith, Prescott, Mark, Veitch, Dallas P.   +3 more
core   +2 more sources