About: Microcalorimetric studies of the interaction mechanisms between proteins and Q-Sepharose at pH near the isoelectric point (pI)

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Microcalorimetric studies of the interaction mechanisms between proteins and Q-Sepharose at pH near the isoelectric point (pI) Goto Sponge NotDistinct Permalink

An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

scientific article published on 01 April 2001

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована у квітні 2001 (uk) im April 2001 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu n'abril de 2001 (ast) scientific article published on 01 April 2001 (en)
publication date	wds:Q57742450-62F3DDCC-FBE6-430E-BC87-17EC2C409D8A
publication date	2001-04-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q57742450-2E0C9032-2421-4861-9144-B1B0890D00D4
language of work or name	English
cites work	wds:Q57742450-02784B59-63EA-424F-AECC-EF0FEBC788AA wds:Q57742450-1AF2CEEB-6FFD-452E-827F-88E94CAC882F wds:Q57742450-2398EC7D-977A-4F4C-92FA-B0F3D9E8A927 wds:Q57742450-4D05DCCA-D2DB-4942-B621-1FF84939BE89 wds:Q57742450-6B1B333B-D5E3-42D5-8168-53A07126BC27 wds:Q57742450-6EC1D839-4941-4BD5-AE39-32051EC618F3 wds:Q57742450-80F33AB9-C254-4AC8-BD39-3C84F0C7B116 wds:Q57742450-84C67DE1-A40A-46BE-8465-2653BE9B5620 wds:Q57742450-96813467-A4AC-4754-9777-D922652B3E59 wds:Q57742450-97CFEFFC-3554-4AF2-8911-84E6AF89EE44 wds:Q57742450-98D1E22E-0529-4DB5-BC32-36FB212576F2 wds:Q57742450-999370DB-7247-418F-8355-05CBE1019797 wds:Q57742450-AE21F79D-A929-4059-9196-A40D4A55F301 wds:Q57742450-C4FB1272-28FE-4086-BCD5-7A895AFA85E5 wds:Q57742450-CAE4B6C1-70E4-4E5A-8BEC-25100B874800 wds:Q57742450-E56CA626-B133-4F05-B502-B71CA0FDDB91
cites work	Selective displacement chromatography of proteins. Microcalorimetric studies of interactions between proteins and hydrophobic ligands in hydrophobic interaction chromatography: effects of ligand chain length, density and the amount of bound protein Adsorption of proteins from solution at the solid-liquid interface Influence of temperature on the retention behaviour of proteins in cation-exchange chromatography Retention behavior of very large biomolecules in ion-exchange chromatography Large-scale Preparation of β-Lactoglobulin A and B by Ultrafiltration and Ion-exchange Chromatography Protein interactions with surface-immobilized metal ions: Structure-dependent variations in affinity and binding capacity with temperature and urea concentration Microcalorimetric characterization of the anion-exchange adsorption of recombinant cytochrome b5 and its surface-charge mutants Ion-exchange chromatography of proteins near the isoelectric points Prediction of protein retention at gradient elution conditions in ion-exchange chromatography Comparative studies on the isothermal characteristics of proteins adsorbed under batch equilibrium conditions to ion-exchange, immobilised metal ion affinity and dye affinity matrices with different ionic strength and temperature conditions. Microcalorimetric Studies of the Interactions of Lysozyme with Immobilized Cu(II): Effects of pH Value and Salt Concentration Microcalorimetric Studies of the Interactions of Lysozyme with Immobilized Metal Ions: Effects of Ion, pH Value, and Salt Concentration Isothermal Titration Microcalorimetric Studies of the Effect of Temperature on Hydrophobic Interaction between Proteins and Hydrophobic Adsorbents High-performance liquid chromatography of amino acids, peptides and proteins. CXXXVIII. Adsorption of horse heart cytochrome c onto a tentacle-type cation exchanger Purification of human adenosine deaminase for the preparation of a reference material
author name string	wds:Q57742450-1AC2AFFB-8B8A-47CD-B9A1-CBAFB38BE3DD wds:Q57742450-205F29A2-78D7-4314-B6D5-75BE584DF40F wds:Q57742450-EE6CC7C1-BC1E-4171-AE6F-E8AD9CBD80F4
author name string	C S Chen W Y Chen F Y Lin
rdfs:label	Microcalorimetric studies of the interaction mechanisms between proteins and Q-Sepharose at pH near the isoelectric point (nl) Microcalorimetric studies of the interaction mechanisms between proteins and Q-Sepharose at pH near the isoelectric point (pI) (en)
skos:prefLabel	Microcalorimetric studies of the interaction mechanisms between proteins and Q-Sepharose at pH near the isoelectric point (nl) Microcalorimetric studies of the interaction mechanisms between proteins and Q-Sepharose at pH near the isoelectric point (pI) (en)
name	Microcalorimetric studies of the interaction mechanisms between proteins and Q-Sepharose at pH near the isoelectric point (nl) Microcalorimetric studies of the interaction mechanisms between proteins and Q-Sepharose at pH near the isoelectric point (pI) (en)
author	wds:Q57742450-71A0D470-C9D3-4F19-8F3E-6E1000BC54E3
author	Shuichi Yamamoto
title	wds:Q57742450-572DF4A1-029A-4DF7-AAA0-C95D44FB1A41
title	Microcalorimetric studies of the interaction mechanisms between proteins and Q-sepharose at pH near the isoelectric point (pI) effects of NaCl concentration, pH value, and temperature (en)
page(s)	wds:Q57742450-3C35ED9A-3138-48C2-999D-1EC136C98237
page(s)	281-289
instance of	wds:Q57742450-C3724270-F6DF-43A6-B264-48DA615E43C0
instance of	scholarly article
PubMed ID	wds:Q57742450-4C222670-549E-4C77-BE22-F0FF29E9FAA6
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11330797
PubMed ID	11330797
published in	wds:Q57742450-7E8CD321-C407-4F71-BAF0-0112B4F8D9D8
published in	Journal of Chromatography
issue	wds:Q57742450-D2CEA132-0BD7-49F9-9F83-527732320313
volume	wds:Q57742450-D798C6D1-36AA-4C90-BBAA-935DA00D7218
issue	2
volume	912
DOI	wds:Q57742450-868CDB53-7891-46CE-864F-D22854DA5718
DOI	http://dx.doi.org/10.1016/S0021-9673(01)00584-2
DOI	10.1016/S0021-9673(01)00584-2
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q57742450
is cites work of	Single and binary adsorption of proteins on ion-exchange adsorbent: The effectiveness of isothermal models. Engineered synthetic polymer nanoparticles as IgG affinity ligands Methods for characterization of biochromatography media Insights into Protein Sorption and Desorption on Dextran-Modified Ion-Exchange Media Influence of pH and ionic strength on the steric mass-action model parameters around the isoelectric point of protein. Fabrication of a Selective and Sensitive Sensor Based on Molecularly Imprinted Polymer/Acetylene Black for the Determination of Azithromycin in Pharmaceuticals and Biological Samples Microcalorimetric studies of the mechanism of interaction between designed peptides and hydrophobic adsorbents Molecular recognition in imprinted polymers: thermodynamic investigation of analyte binding using microcalorimetry Thermodynamic analysis of the interaction between proteins and solid surfaces: application to liquid chromatography Reactions between bacterial exopolymers and goethite: A combined macroscopic and spectroscopic investigation. Studies on the binding sites of IgG2 monoclonal antibodies recognized by terpyridine-based affinity ligands. Pressure-induced effects in the heterogeneous adsorption of insulin on chromatographic surfaces Microcalorimetric studies of the effects on the interactions of human recombinant interferon-alpha2a Hydrophobic interaction chromatography of proteins: Studies of unfolding upon adsorption by isothermal titration calorimetry
is cites work of	wds:Q38056668-EDB8587C-C6A6-403C-94BE-E6B58E93D630 wds:Q36351140-79B4AF6F-3683-4B5E-B65F-FEC674E7959D wds:Q35907167-E3168BB6-25D1-49F6-8DCD-E7981317C6A6 wds:Q51329987-FBB991B6-A6F8-457F-B0F8-C7E750F37B7A wds:Q34601784-21F9346B-EA11-4A8E-978B-50FF5AB0B86C wds:Q43710929-9E4D1C28-7CDB-4AC3-9870-4B3524843A46 wds:Q47431959-03ECCE69-2363-4460-9691-44983D0E66BF wds:Q47270693-A1E8D8D0-9028-4800-809B-747A6395B230 wds:Q40026405-274152F1-4E3B-4395-B760-A08D93FD5289 wds:Q81561754-DBB14143-0DD7-406B-9393-2A3887305B5F wds:Q51514727-0A5B5A4E-B9D5-4D37-8340-03D37DABEA75

Faceted Search & Find service v1.16.117 as of May 05 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3239 as of May 5 2024, on Linux (x86_64-centos_6-linux-gnu), Single-Server Edition (378 GB total memory, 180 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2025 OpenLink Software