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Please use this identifier to cite or link to this item: http://dspace.bits-pilani.ac.in:8080/jspui/handle/123456789/19006
Title: Enthalpy of Interaction between some Globular Proteins and Sodium n-Dodecyl Sulphate in Aqueous Solution
Authors: Tipping, Edward
Jones, Malcolm N.
Skinner, Henry A.
Keywords: Chemistry
Enthalpy of Interaction
Globular Proteins
Journal of the Chemical Society : Faraday Transaction - I
Issue Date: 1974
Publisher: Journal of the Chemical Society : Faraday Transaction - I. The Chemical Society, London. 1974, 70 (07)
Abstract: The enthalpy of binding of sodium n-dodecyl sulphate (SDS) to scrum albumin, ovalbumin and ribonuclease A has been measured by microcalorimetry over the temperature range 18.5 to 32.0 C. The amount of SDS bound to the proteins has been measured over a wide range of SDS concentration by equilibrium dialysis. Changes in protein conformation have been monitored by viscometry. The results are consistent with a mechanism in which SDS binds initially to ionic sites on the protein molecules and initiates chain unfolding. At high binding levels the interaction is predominantly of a hydrophobic nature.
URI: http://dspace.bits-pilani.ac.in:8080/jspui/handle/123456789/19006
Appears in Collections:Journal Articles (before-1995)

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