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Studies of binding by macromolecules: A new dialysis technique for obtaining quantitative data

✍ Scribed by Herman H. Stein

Publisher
Elsevier Science
Year
1965
Tongue
English
Weight
438 KB
Volume
13
Category
Article
ISSN
0003-2697

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✦ Synopsis

Equilibrium

dialysis (1, 2) is a proved technique for obtaining quantitative data concerning the reversible interaction between a dialyzable species and a macromolecule.

Upon proper treatment of the binding data, it is possible to determine the equilibrium constant for the formation of the complex and to estimate the number of sites on the macromolecule to which the small species is bound (3-5).

A significant disadvantage of the experimental procedure is the long periods of time required for attainment of equilibrium.

Frequently, periods of 24 hr or more are involved, and if a labile material is being studied decomposition products can yield misleading results.

The purpose of this paper is to describe a dynamic dialysis technique which yields the same information as the classical procedure, but which requires only minutes to perform since equilibrium is not required. Used in conjunction with an automatic analytical system, it is possible to generate the requisite data for a complete binding profile within an S-hr period.

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