3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate has been researched along with sarcosine in 5 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 1 (20.00) | 29.6817 |
| 2010's | 4 (80.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Gai, WP; Lowe, R; Pountney, DL; Quilty, M; Vickers, JC; Voelcker, NH | 1 |
| Cox, TC; Harris, HK; Liu, W; Massiah, MA; Simmons, BN; Tao, H | 1 |
| de Los Ángeles Camacho-Ruiz, M; Mateos-Díaz, E; Mateos-Díaz, JC; Rodríguez, JA | 1 |
| Du, H; Massiah, MA; Wright, KM | 1 |
| Béven, L; Desfougères, Y; Poitou, JM; Wróblewski, H | 1 |
5 other study(ies) available for 3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate and sarcosine
| Article | Year |
|---|---|
Annular alpha-synuclein species from purified multiple system atrophy inclusions.
Topics: alpha-Synuclein; Brain Chemistry; Cholic Acids; Detergents; Humans; Inclusion Bodies; Macromolecular Substances; Microscopy, Atomic Force; Microscopy, Electron, Scanning; Molecular Weight; Multiple System Atrophy; Nerve Tissue Proteins; Oligodendroglia; Particle Size; Recombinant Proteins; Sarcosine; Synucleins | 2004 |
Purifying natively folded proteins from inclusion bodies using sarkosyl, Triton X-100, and CHAPS.
Topics: Cholic Acids; Escherichia coli; Glutathione Transferase; Inclusion Bodies; Maltose-Binding Proteins; Octoxynol; Periplasmic Binding Proteins; Protein Folding; Recombinant Fusion Proteins; Sarcosine; Solubility | 2010 |
High-throughput screening method for lipases/esterases.
Topics: Bacterial Proteins; beta-Cyclodextrins; Caprylates; Cholic Acids; Esterases; Fungal Proteins; High-Throughput Screening Assays; Hydrogen-Ion Concentration; Hydrolysis; Kinetics; Lipase; Octoxynol; Sarcosine; Substrate Specificity; Triglycerides | 2012 |
Obtaining Soluble Folded Proteins from Inclusion Bodies Using Sarkosyl, Triton X-100, and CHAPS: Application to LB and M9 Minimal Media.
Topics: Betaine; Cholic Acids; Escherichia coli; Glutathione Transferase; Histidine; Inclusion Bodies; Octoxynol; Protein Engineering; Protein Folding; Recombinant Fusion Proteins; Recombinant Proteins; Sarcosine; Solubility; Sorbitol | 2016 |
An improved non-denaturing method for the purification of spiralin, the main membrane lipoprotein of the pathogenic bacteria Spiroplasma melliferum.
Topics: Bacterial Outer Membrane Proteins; Cholic Acids; Chromatography, Gel; Chromatography, High Pressure Liquid; Chromatography, Ion Exchange; Circular Dichroism; Detergents; Protein Conformation; Protein Denaturation; Sarcosine; Spiroplasma | 2016 |