Analysis of protein association by partitioning in aqueous two-phase polymer systems: Applications to the tetramer-dimer dissociation of hemoglobin

✍ Scribed by C. Russell Middaugh; Erlinda Q. Lawson

• Publisher: Elsevier Science
• Year: 1980
• Tongue: English
• Weight: 356 KB
• Volume: 105
• Category: Article
• ISSN: 0003-2697
• DOI: 10.1016/0003-2697(80)90471-6

✦ Synopsis

A new simple and rapid method for the determination of protein-protein association constants is described. By maximizing experimental conditions in which size becomes the controlling variable, analysis of the effect of protein concentration on the partitioning behavior of proteins in aqueous two-phase polymer systems permits an accurate estimate of protein association constants. When employed to investigate the tetramer-dimer dissociation of human oxy-and methemoglobin in the presence and absence of high salt concentration, values for the dissociation constant are obtained that are consistent with those obtained by other methods.

Methods

Human hemoglobin was purified as described previously (3) and stored in the cold