Horseradish peroxidase extraction and purification by aqueous two-phase partition
✍ Scribed by Mar’ia V. Miranda; H’ector m. Fern’andez Lahore; Osvaldo Cascone
- Book ID
- 112894169
- Publisher
- Springer-Verlag
- Year
- 1995
- Tongue
- English
- Weight
- 380 KB
- Volume
- 53
- Category
- Article
- ISSN
- 0273-2289
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Partition of purified horseradish peroxidase isoenzymes in aqueous two-phase systems was not affected by pH changes, but tie-line length and NaCl addition greatly increased the partition coefficient of ail three isoenzymes, the former having more influence than the latter. In all systems, K were hig
Amino acids, including lysine, glutamic acid, and phenylalanine, in pure solution or in fermentation broth, were extracted with the aqueous two-phase system consisting of polyethylene glycol and salts, giving a very sharp separation. The partition is influenced by the type and the amount of salts us
## Abstract Countercurrent chromatography (CCC) purification of horseradish peroxidase (HRP) from __Armoracia rusticana__ root extracts was achieved by employing polymer‐phosphate aqueous two‐phase systems (ATPS). By using preparative columns at 1000 rpm, a 25–30% retention of the top phase of an A