perature for 10 min. The DTT was removed by extraction with 400 lL ethylacetate. The resulting aqueous solution was diluted to create a 1 lM solution in 1 M potassium phosphate buffer pH 7.0. The DNA linker solution was mixed with a 1 lM solution of 6-mercapto-1-hexanol in 1 M potassium phosphate bu
Effects of solutions used for storage of size-exclusion columns on subsequent chromatography of peptides and proteins
β Scribed by G.W. Link Jr.; P.L. Keller; R.W. Stout; A.J. Banes
- Publisher
- Elsevier Science
- Year
- 1985
- Tongue
- English
- Weight
- 794 KB
- Volume
- 331
- Category
- Article
- ISSN
- 1873-3778
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
## Abstract Arsenicβbinding proteins are of toxicological importance since enzymatic activities can be blocked by arsenic interactions. In the present work, a novel methodology based on size exclusion chromatography coupled to electrospray ionization mass spectrometry (SECβESIβMS) was developed wit
Trifluoroacetic acid (0.1% w/v) is an excellent solvent for polypeptides, is volatile, and has a low absorbance of ultraviolet light of low wavelength. Polypeptides subjected to chromatography on columns of TSK-G2000-SW or TSK-G3000-SW in this solvent were eluted as sharp peaks. Retention volume was
A peptide fragment corresponding to the third helix of Staphylococcus Aureus protein A, domain B, was chosen to study the effect of the main-chain direction upon secondary structure formation and stability, applying the retro-enantio concept. For this purpose, two peptides consisting of the native (