Matches in SemOpenAlex for { <https://semopenalex.org/work/W1995511258> ?p ?o ?g. }
Showing items 1 to 95 of
95
with 100 items per page.
- W1995511258 endingPage "280" @default.
- W1995511258 startingPage "273" @default.
- W1995511258 abstract "Notwithstanding the use of acidic, amphoteric, isoelectric buffers with isoelectric points (pI) in the pH 2–3 range, adsorption of proteins to the naked silica wall can be non-negligible. Two such buffers have been tested: iminodiacetic acid (IDA; pI 2.23, apparent pH 3.2 in 7 M urea) and aspartic acid (pI 2.77, apparent pH 3.7 in 7 M urea). Three potential quenchers of such interactions have been tested: hydroxyethylcellulose (HEC; number average molecular mass, Mr 27 000), TEPA (tetraethylenepentamine) and a novel, quaternarized piperazine [N(methyl-N-ω-iodobutyl)-N′-methylpiperazine] (Q-Pip), either alone or in binary and ternary mixtures. Human α- and β-globin chains have been used as test proteins in capillary electrophoresis separations. It has been found that mixtures of these compounds are the worst possible remedy. E.g., a ternary mixture comprising 0.5% HEC, 0.5 mM TEPA and 1 mM Q-Pip still leaves behind 4.5% adsorbed protein onto the silica surface in runs in IDA buffer and 7 M urea (pH 3.2). Conversely, 0.5 mM TEPA or 1 mM Q-Pip, when used alone, minimize adsorption down to only 1.8% and 0.5%, respectively. When the same globin chain separations are performed in Asp and 7 M urea (pH 3.7), the situation is much worse: 44% protein is adsorbed in a ternary mixture of 0.5% HEC, 1 mM Q-Pip and 0.5 mM TEPA. However, when used alone, 0.5 mM TEPA and 1 mM Q-Pip reduce globin adsorption to levels of 8% and 5%, respectively. TEPA and Q-Pip are found to be in all cases the best quenchers of protein interaction to naked fused-silica; in addition they exhibit the unique property of smoothing the base-line and giving reproducible runs. The best method for desorbing bound protein was found to be an electrophoretic step consisting in driving sodium dodecylsulphate micelles from the cathodic reservoir." @default.
- W1995511258 created "2016-06-24" @default.
- W1995511258 creator A5001369117 @default.
- W1995511258 creator A5025798621 @default.
- W1995511258 creator A5060277927 @default.
- W1995511258 creator A5074843073 @default.
- W1995511258 creator A5089515036 @default.
- W1995511258 date "2000-10-01" @default.
- W1995511258 modified "2023-10-13" @default.
- W1995511258 title "Quantitation of protein binding to the capillary wall in acidic, isoelectric buffers and means for minimizing the phenomenon" @default.
- W1995511258 cites W162472049 @default.
- W1995511258 cites W1970333261 @default.
- W1995511258 cites W1976582011 @default.
- W1995511258 cites W1989614327 @default.
- W1995511258 cites W1995591012 @default.
- W1995511258 cites W2014886142 @default.
- W1995511258 cites W2025449910 @default.
- W1995511258 cites W2030907570 @default.
- W1995511258 cites W2041549174 @default.
- W1995511258 cites W2047173571 @default.
- W1995511258 cites W2074474136 @default.
- W1995511258 cites W2076927196 @default.
- W1995511258 cites W2080406238 @default.
- W1995511258 cites W2088768065 @default.
- W1995511258 cites W2089769569 @default.
- W1995511258 cites W2090527886 @default.
- W1995511258 cites W4231275087 @default.
- W1995511258 doi "https://doi.org/10.1016/s0021-9673(00)00665-8" @default.
- W1995511258 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11100870" @default.
- W1995511258 hasPublicationYear "2000" @default.
- W1995511258 type Work @default.
- W1995511258 sameAs 1995511258 @default.
- W1995511258 citedByCount "42" @default.
- W1995511258 countsByYear W19955112582016 @default.
- W1995511258 countsByYear W19955112582017 @default.
- W1995511258 crossrefType "journal-article" @default.
- W1995511258 hasAuthorship W1995511258A5001369117 @default.
- W1995511258 hasAuthorship W1995511258A5025798621 @default.
- W1995511258 hasAuthorship W1995511258A5060277927 @default.
- W1995511258 hasAuthorship W1995511258A5074843073 @default.
- W1995511258 hasAuthorship W1995511258A5089515036 @default.
- W1995511258 hasConcept C150394285 @default.
- W1995511258 hasConcept C178790620 @default.
- W1995511258 hasConcept C179104552 @default.
- W1995511258 hasConcept C181199279 @default.
- W1995511258 hasConcept C185592680 @default.
- W1995511258 hasConcept C197404232 @default.
- W1995511258 hasConcept C199360897 @default.
- W1995511258 hasConcept C2780365088 @default.
- W1995511258 hasConcept C2781137352 @default.
- W1995511258 hasConcept C2900643 @default.
- W1995511258 hasConcept C40250595 @default.
- W1995511258 hasConcept C41008148 @default.
- W1995511258 hasConcept C43617362 @default.
- W1995511258 hasConcept C50476208 @default.
- W1995511258 hasConcept C64452783 @default.
- W1995511258 hasConcept C96294017 @default.
- W1995511258 hasConceptScore W1995511258C150394285 @default.
- W1995511258 hasConceptScore W1995511258C178790620 @default.
- W1995511258 hasConceptScore W1995511258C179104552 @default.
- W1995511258 hasConceptScore W1995511258C181199279 @default.
- W1995511258 hasConceptScore W1995511258C185592680 @default.
- W1995511258 hasConceptScore W1995511258C197404232 @default.
- W1995511258 hasConceptScore W1995511258C199360897 @default.
- W1995511258 hasConceptScore W1995511258C2780365088 @default.
- W1995511258 hasConceptScore W1995511258C2781137352 @default.
- W1995511258 hasConceptScore W1995511258C2900643 @default.
- W1995511258 hasConceptScore W1995511258C40250595 @default.
- W1995511258 hasConceptScore W1995511258C41008148 @default.
- W1995511258 hasConceptScore W1995511258C43617362 @default.
- W1995511258 hasConceptScore W1995511258C50476208 @default.
- W1995511258 hasConceptScore W1995511258C64452783 @default.
- W1995511258 hasConceptScore W1995511258C96294017 @default.
- W1995511258 hasIssue "1-2" @default.
- W1995511258 hasLocation W19955112581 @default.
- W1995511258 hasLocation W19955112582 @default.
- W1995511258 hasOpenAccess W1995511258 @default.
- W1995511258 hasPrimaryLocation W19955112581 @default.
- W1995511258 hasRelatedWork W109922730 @default.
- W1995511258 hasRelatedWork W115908265 @default.
- W1995511258 hasRelatedWork W1967452203 @default.
- W1995511258 hasRelatedWork W1970374638 @default.
- W1995511258 hasRelatedWork W1982499865 @default.
- W1995511258 hasRelatedWork W2080913337 @default.
- W1995511258 hasRelatedWork W2081064559 @default.
- W1995511258 hasRelatedWork W2110477250 @default.
- W1995511258 hasRelatedWork W2131261912 @default.
- W1995511258 hasRelatedWork W3161861076 @default.
- W1995511258 hasVolume "894" @default.
- W1995511258 isParatext "false" @default.
- W1995511258 isRetracted "false" @default.
- W1995511258 magId "1995511258" @default.
- W1995511258 workType "article" @default.