## Abstract Reversed phase microcolumn (0.32 mm i.d.) liquid chromatography was used to purify low‐picomole amounts of proteins and peptides suitable for structural analysis. Using this approach, rapid trace enrichment (concentration) of low nanogram levels of proteins from volumes as high as 500 μ
Tryptophan analysis in peptides and proteins, mainly by liquid chromatography
✍ Scribed by Ibolya Molnár-Perl
- Book ID
- 108340900
- Publisher
- Elsevier Science
- Year
- 1997
- Tongue
- English
- Weight
- 746 KB
- Volume
- 763
- Category
- Article
- ISSN
- 1873-3778
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This report describes the use of hydrophobic ion-pairing reagents in the rapid analysis of peptides by reversed-phase high-pressure liquid chromatography. It was found that combination of a hydrophobic anion such as hexanesulphonate with the c&ionic groups (R&H,) of a peptide resulted in a decreased
Proteins and peptides were separated in the reversed-phase mode on microcolumns packed with nonporous octadecyl-group bonded silica gel with an average particle diameter of 4.5 or 20 pm. Separation columns were prepared from glass-lined stainless steel tubing of 39 or 56-mm x 0.5-mm i.d. An artifici