scholarly journals Avoiding Proteolysis During Protein Chromatography

2010 ◽  
pp. 61-71 ◽  
Author(s):  
Barry J. Ryan
Keyword(s):  
Protein Chromatography

Optimization of elution salt concentration in stepwise elution of protein chromatography using linear gradient elution data

2006 ◽  
Vol 1114 (1) ◽  
pp. 97-101 ◽  
Author(s):  
Takashi Ishihara ◽  
Toshihiko Kadoya ◽  
Naomi Endo ◽  
Shuichi Yamamoto
Keyword(s):  
Salt Concentration ◽  
Gradient Elution ◽  
Linear Gradient ◽  
Protein Chromatography

Microbore flow-rates and protein chromatography

1987 ◽  
Vol 385 ◽  
pp. 65-74 ◽  
Author(s):  
Timothy D. Schlabach ◽  
Kenneth J. Wilson
Keyword(s):  
Flow Rates ◽  
Protein Chromatography

scholarly journals A Facile Way for Preparation of Cellulose Beads With High Homogeneity, Low Crystallinity, and Tunable - Internal Structure

2021 ◽  
Author(s):  
Yuanyuan Xia ◽  
Xinping Li ◽  
Yue Yuan ◽  
Jingshun Zhuang ◽  
Wenliang Wang
Keyword(s):  
Crystal Form ◽  
Energy Storage Materials ◽  
Regenerated Cellulose ◽  
Protein Chromatography ◽  
Green Materials ◽  
Coagulation Mechanism ◽  
Structures And Properties ◽  
Water Holding ◽  
Water Alcohol ◽  
Low Crystallinity

Abstract The preparation of cellulose beads has attracted more and more attention in the application of advanced green materials. To obtain uniform and controllable cellulose beads, the dissolving pulp was dissolved in NMMO, and the cellulose beads were regenerated in various coagulation baths (water, alcohol, acid, NMMO, etc.) by phase conversion method. Results show that the crystal form of regenerated cellulose changes from cellulose I to cellulose II. NMMO swelling cellulose beads present low crystallinity and low water holding capacity. The coagulation mechanism of cellulose beads was clarified by a laser confocal microscopy. It is found that the whole coagulation process was from outside to inside gradually. It is a green and facile method for preparing cellulose beads with different structures and properties, which can be widely used in biomedicine, energy storage materials, and protein chromatography.

Protein Stable Isotope Fingerprinting: Multidimensional Protein Chromatography Coupled to Stable Isotope-Ratio Mass Spectrometry

2014 ◽  
Vol 86 (17) ◽  
pp. 8514-8520 ◽  
Author(s):  
Wiebke Mohr ◽  
Tiantian Tang ◽  
Sarah R. Sattin ◽  
Roderick J. Bovee ◽  
Ann Pearson
Keyword(s):  
Mass Spectrometry ◽  
Stable Isotope ◽  
Isotope Ratio ◽  
Isotope Ratio Mass Spectrometry ◽  
Stable Isotope Ratio ◽  
Protein Chromatography

scholarly journals Protein chromatography on adsorbents with hydrophobic and ionic groups. Purification of human erythrocyte glycophorin

1977 ◽  
Vol 163 (2) ◽  
pp. 397-400 ◽  
Author(s):  
R J Simmonds ◽  
R J Yon
Keyword(s):  
Sodium Dodecyl Sulphate ◽  
Human Erythrocyte ◽  
Sodium Dodecyl ◽  
Erythrocyte Ghosts ◽  
Electrophoretic Band ◽  
Protein Chromatography ◽  
Ionic Groups ◽  
A Subunit ◽  
Triton X

Human erythrocyte glycophorin was purified rapidly by (a) chromatography of a Triton X-100 extract of erythrocyte ‘ghosts’ on N-(3-carboxypropionyl)aminodecyl-Sepharose in buffers containing Triton X-100 or sodium dodecyl sulphate, or (b) chromatography of whole ‘ghosts’, solubilized in sodium dodecyl sulphate, on dodecyl-Sepharose, in buffers containing sodium dodecyl sulphate. The products contained 85-95% glycophorin (electrophoretic band PAS-1) and the major contaminants were glycoproteins PAS-2 (possibly a subunit of glycophorin) and PAS-3.

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