𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Hydrophobic surface properties of myosin in solution as studied by partition in aqueous two-phase systems: effects of ionic strength, pH and temperature

✍ Scribed by G. Pinaev; A. Tartakovsky; V. P. Shanbhag; G. Johansson; L. Backman


Publisher
Springer
Year
1982
Tongue
English
Weight
292 KB
Volume
48
Category
Article
ISSN
0300-8177

No coin nor oath required. For personal study only.


πŸ“œ SIMILAR VOLUMES


Correlation for the partition behavior o
✍ B.A. Andrews; A.S. Schmidt; J.A. Asenjo πŸ“‚ Article πŸ“… 2005 πŸ› John Wiley and Sons 🌐 English βš– 566 KB

## Abstract Correlations to describe the effect of surface hydrophobicity and charge of proteins with their partition coefficient in aqueous two‐phase systems were investigated. Polyethylene glycol (PEG) 4000/phosphate, sulfate, citrate, and dextran systems in the presence of low (0.6% w/w) and hig

Use of chemically modified proteins to s
✍ T. T. Franco; A. T. Andrews; J. A. Asenjo πŸ“‚ Article πŸ“… 2000 πŸ› John Wiley and Sons 🌐 English βš– 867 KB

Two different series of hydrophobically modified proteins were partitioned in a number of aqueous two-phase systems (ATPS) to investigate the effect of hydrophobicity as a single property on partitioning. The modified proteins were derived from P-lactoglobulin and bovine serum albumin (BSA). Measure