Hydrophobic surface properties of myosin in solution as studied by partition in aqueous two-phase systems: effects of ionic strength, pH and temperature
β 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
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## Abstract Correlations to describe the effect of surface hydrophobicity and charge of proteins with their partition coefficient in aqueous twoβphase systems were investigated. Polyethylene glycol (PEG) 4000/phosphate, sulfate, citrate, and dextran systems in the presence of low (0.6% w/w) and hig
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